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		<title>3j5l - Revision history</title>
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			<title>OCA at 14:15, 24 January 2024</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=4029587&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 14:15, 24 January 2024&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;33 &lt;/del&gt;chain structure with sequence from [https://en.wikipedia.org/wiki/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Escherichia_coli &lt;/del&gt;Escherichia coli] and [https://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [https://proteopedia.org/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;10 &lt;/ins&gt;chain structure with sequence from [https://en.wikipedia.org/wiki/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Escherichia_coli_K-12 &lt;/ins&gt;Escherichia coli &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;K-12&lt;/ins&gt;] and [https://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [https://proteopedia.org/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ligand&lt;/del&gt;'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Ligand&lt;/del&gt;|&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Ligands&lt;/del&gt;:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot; id=&amp;quot;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ligandDat&lt;/del&gt;&amp;quot;&amp;gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;&lt;/del&gt;, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&lt;/del&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;method&lt;/ins&gt;'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Empirical_models&lt;/ins&gt;|&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Method&lt;/ins&gt;:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot; id=&amp;quot;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;methodDat&lt;/ins&gt;&amp;quot;&amp;gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Electron Microscopy&lt;/ins&gt;, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Resolution|Resolution]] 6.6&amp;amp;#8491;&lt;/ins&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;NonStdRes&lt;/del&gt;'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Non-Standard_Residue&lt;/del&gt;|&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;NonStd Res&lt;/del&gt;:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ligand&lt;/ins&gt;'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Ligand&lt;/ins&gt;|&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Ligands&lt;/ins&gt;:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;quot; id=&amp;quot;ligandDat&lt;/ins&gt;&amp;quot;&amp;gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &lt;/ins&gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&lt;/ins&gt;&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[https://proteopedia.org/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [https://pdbe.org/3j5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [https://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[https://proteopedia.org/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [https://pdbe.org/3j5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [https://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[https://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [&lt;/del&gt;[https://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]&lt;/del&gt;] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[https://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[https://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[https://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[https://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[https://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[https://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[https://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[https://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[https://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[https://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[https://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[https://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[https://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[https://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[https://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[https://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[https://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[https://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[https://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[https://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 23:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 23:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;__TOC__&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;__TOC__&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/SX&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/SX&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;K-12&lt;/ins&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Large Structures]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Large Structures]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;S]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz S]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Beckmann&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;R]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Beckmann R]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Berninghausen&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;O]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Berninghausen O]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Gupta&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;P]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Gupta P]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Mankin&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, A S&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Mankin &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;AS&lt;/ins&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ramu&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;H]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ramu H]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Vazquez-Laslop&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;N]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Vazquez-Laslop N]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Wilson&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, D N]]&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Wilson &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;DN&lt;/ins&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Erythromycin]]&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Ribosome-antibiotic complex]]&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Stalling&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 24 Jan 2024 14:15:53 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 03:50, 21 April 2022</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=3550172&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 03:50, 21 April 2022&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://proteopedia.org/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://proteopedia.org/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot; id=&amp;quot;ligandDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot; id=&amp;quot;ligandDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://proteopedia.org/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://pdbe.org/3j5l PDBe], [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://proteopedia.org/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://pdbe.org/3j5l PDBe], [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;http&lt;/del&gt;://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;https&lt;/ins&gt;://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
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			<pubDate>Thu, 21 Apr 2022 03:50:12 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
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			<title>OCA at 17:57, 10 April 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=3186673&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 17:57, 10 April 2020&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 3:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;SX load='3j5l' size='340' side='right' viewer='molstar' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;oca&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;weizmann.ac.il/oca-docs&lt;/del&gt;/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteopedia&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org&lt;/ins&gt;/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;quot; id=&amp;quot;ligandDat&lt;/ins&gt;&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;oca&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;weizmann.ac.il/oca-docs&lt;/del&gt;/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://pdbe.org/3j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteopedia&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org&lt;/ins&gt;/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://pdbe.org/3j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Fri, 10 Apr 2020 17:57:14 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 17:24, 6 March 2020</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=3166839&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 17:24, 6 March 2020&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{Large structure}}&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection &lt;/del&gt;load='3j5l' size='340' side='right' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;SX &lt;/ins&gt;load='3j5l' size='340' side='right&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;' viewer='molstar&lt;/ins&gt;' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Structural highlights ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://pdbe.org/3j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://pdbe.org/3j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{Large structure}}&lt;/div&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL15_ECOLI RL15_ECOLI&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;This protein binds the 5S rRNA. It is required for the late stages &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit &lt;/del&gt;assembly, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and is essential for 5S &lt;/del&gt;rRNA assembly &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;onto &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01341_B&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL19_ECOLI RL19_ECOLI&lt;/del&gt;]] This protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;is located &lt;/del&gt;at the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S-50S &lt;/del&gt;ribosomal &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit interface&lt;/del&gt;. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S &lt;/del&gt;subunit &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near &lt;/del&gt;the base of the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L1 &lt;/del&gt;stalk, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;it is probably also mobile. Required for association of the 30S &lt;/del&gt;and &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S subunits to form &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S ribosome, for &lt;/del&gt;tRNA binding &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and peptide bond formation. It has been suggested to have &lt;/del&gt;peptidyltransferase &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;activity; this is highly controversial&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01320_B&lt;/del&gt;]  &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In the E.coli 70S ribosome &lt;/del&gt;in &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01320_B&lt;/del&gt;] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL17_ECOLI RL17_ECOLI&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this &lt;/del&gt;protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;initially &lt;/del&gt;binds &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;near &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5'-end of the 23S &lt;/del&gt;rRNA. It is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;important during &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;early &lt;/del&gt;stages of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S &lt;/del&gt;assembly&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit &lt;/del&gt;and &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 &lt;/del&gt;is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required &lt;/del&gt;for &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome &lt;/del&gt;assembly &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;polypeptide exit tunnel&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  &lt;/del&gt;[[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL18_ECOLI RL18_ECOLI&lt;/del&gt;]] This is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;one of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteins that mediates the attachment of the 5S rRNA subcomplex onto the large &lt;/del&gt;ribosomal subunit &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;where it forms part of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of &lt;/del&gt;ribosome&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;-bound tRNAs.&amp;lt;ref&amp;gt;PMID&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, &lt;/del&gt;it &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly &lt;/del&gt;to the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5'-end of the 23S &lt;/del&gt;rRNA&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates assembly &lt;/del&gt;of the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S &lt;/del&gt;subunit&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. It is not thought to be involved in the functions &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the mature 50S subunit in vitro&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteins that surrounds the polypeptide exit tunnel on the outside of the subunit&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;3'-end of the 23S &lt;/del&gt;rRNA&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates assembly of the 50S subunit&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This &lt;/del&gt;protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly to at least 2 domains of the 23S ribosomal RNA, thus &lt;/del&gt;is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;important in its secondary structure. It is located near &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit interface in the base of the L7/L12 stalk&lt;/del&gt;, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and near the tRNA binding site of the peptidyltransferase center&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  &lt;/ins&gt;[[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  &lt;/ins&gt;[[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL3_ECOLI RL3_ECOLI&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;One &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;two &lt;/ins&gt;assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;inititator proteins&lt;/ins&gt;, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;it binds directly near the 3'-end of the 23S &lt;/ins&gt;rRNA&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates &lt;/ins&gt;assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S subunit&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01325_B&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL6_ECOLI RL6_ECOLI&lt;/ins&gt;]] This protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly to &lt;/ins&gt;at &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;least 2 domains of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;23S &lt;/ins&gt;ribosomal &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RNA, thus is important in its secondary structure&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;It is located near &lt;/ins&gt;the subunit &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;interface in &lt;/ins&gt;the base of the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L7/L12 &lt;/ins&gt;stalk, and &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;near &lt;/ins&gt;the tRNA binding &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;site of the &lt;/ins&gt;peptidyltransferase &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;center&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365&lt;/ins&gt;]  &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Gentamicin-resistant mutations &lt;/ins&gt;in &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;this protein affect translation fidelity&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL15_ECOLI RL15_ECOLI&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;This &lt;/ins&gt;protein binds the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5S &lt;/ins&gt;rRNA. It is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;required for &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;late &lt;/ins&gt;stages of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit &lt;/ins&gt;assembly&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/ins&gt;and is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;essential &lt;/ins&gt;for &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5S rRNA &lt;/ins&gt;assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;onto &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[HAMAP-Rule&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01341_B] &lt;/ins&gt;[[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL19_ECOLI RL19_ECOLI&lt;/ins&gt;]] This &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;protein &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;located at &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S-50S &lt;/ins&gt;ribosomal subunit &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;interface. In &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S &lt;/ins&gt;ribosome &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(PubMed&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;12809609) &lt;/ins&gt;it &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;has been modeled &lt;/ins&gt;to &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;make two contacts with &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16S &lt;/ins&gt;rRNA of the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S &lt;/ins&gt;subunit &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;forming part &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;bridges B6 and B8&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;3&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5 A resolved structures (PubMed&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16272117) L14 and L19 interact and together make contact with &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16S &lt;/ins&gt;rRNA. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;The &lt;/ins&gt;protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;conformation &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;quite different between &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S and 70S structures&lt;/ins&gt;, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;which may be necessary for translocation&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_00402&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 23:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 22:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;__TOC__&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;__TOC__&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection&lt;/del&gt;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;SX&lt;/ins&gt;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Large Structures]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz, S]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz, S]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Fri, 06 Mar 2020 17:24:10 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 08:12, 18 July 2018</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=2925430&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 08:12, 18 July 2018&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 10:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 10:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{Large structure}}&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{Large structure}}&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  &lt;/del&gt;[[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  &lt;/del&gt;[[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL3_ECOLI RL3_ECOLI&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;One &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;two &lt;/del&gt;assembly &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;inititator proteins&lt;/del&gt;, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;it binds directly near the 3'-end of the 23S &lt;/del&gt;rRNA&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates &lt;/del&gt;assembly &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S subunit&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01325_B&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL6_ECOLI RL6_ECOLI&lt;/del&gt;]] This protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly to &lt;/del&gt;at &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;least 2 domains of &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;23S &lt;/del&gt;ribosomal &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RNA, thus is important in its secondary structure&lt;/del&gt;. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;It is located near &lt;/del&gt;the subunit &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;interface in &lt;/del&gt;the base of the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L7/L12 &lt;/del&gt;stalk, and &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;near &lt;/del&gt;the tRNA binding &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;site of the &lt;/del&gt;peptidyltransferase &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;center&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365&lt;/del&gt;]  &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Gentamicin-resistant mutations &lt;/del&gt;in &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;this protein affect translation fidelity&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365&lt;/del&gt;] [[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL15_ECOLI RL15_ECOLI&lt;/del&gt;]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;This &lt;/del&gt;protein binds the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5S &lt;/del&gt;rRNA. It is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;required for &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;late &lt;/del&gt;stages of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit &lt;/del&gt;assembly&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/del&gt;and is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;essential &lt;/del&gt;for &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5S rRNA &lt;/del&gt;assembly &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;onto &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[HAMAP-Rule&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01341_B] &lt;/del&gt;[[http://www.uniprot.org/uniprot/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL19_ECOLI RL19_ECOLI&lt;/del&gt;]] This &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;protein &lt;/del&gt;is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;located at &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S-50S &lt;/del&gt;ribosomal subunit &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;interface. In &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S &lt;/del&gt;ribosome &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(PubMed&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;12809609) &lt;/del&gt;it &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;has been modeled &lt;/del&gt;to &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;make two contacts with &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16S &lt;/del&gt;rRNA of the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S &lt;/del&gt;subunit &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;forming part &lt;/del&gt;of &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;bridges B6 and B8&lt;/del&gt;. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;3&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5 A resolved structures (PubMed&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16272117) L14 and L19 interact and together make contact with &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;16S &lt;/del&gt;rRNA. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;The &lt;/del&gt;protein &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;conformation &lt;/del&gt;is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;quite different between &lt;/del&gt;the &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S and 70S structures&lt;/del&gt;, &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;which may be necessary for translocation&lt;/del&gt;.[HAMAP-Rule:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_00402&lt;/del&gt;] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL15_ECOLI RL15_ECOLI&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;This protein binds the 5S rRNA. It is required for the late stages &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit &lt;/ins&gt;assembly, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and is essential for 5S &lt;/ins&gt;rRNA assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;onto &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01341_B&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL19_ECOLI RL19_ECOLI&lt;/ins&gt;]] This protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;is located &lt;/ins&gt;at the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;30S-50S &lt;/ins&gt;ribosomal &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit interface&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S &lt;/ins&gt;subunit &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near &lt;/ins&gt;the base of the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;L1 &lt;/ins&gt;stalk, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;it is probably also mobile. Required for association of the 30S &lt;/ins&gt;and &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S subunits to form &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;70S ribosome, for &lt;/ins&gt;tRNA binding &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and peptide bond formation. It has been suggested to have &lt;/ins&gt;peptidyltransferase &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;activity; this is highly controversial&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01320_B&lt;/ins&gt;]  &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;In the E.coli 70S ribosome &lt;/ins&gt;in &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01320_B&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL17_ECOLI RL17_ECOLI&lt;/ins&gt;]] &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this &lt;/ins&gt;protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;initially &lt;/ins&gt;binds &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;near &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5'-end of the 23S &lt;/ins&gt;rRNA. It is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;important during &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;early &lt;/ins&gt;stages of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S &lt;/ins&gt;assembly&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit &lt;/ins&gt;and &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required &lt;/ins&gt;for &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ribosome &lt;/ins&gt;assembly &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;(residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;polypeptide exit tunnel&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  &lt;/ins&gt;[[http://www.uniprot.org/uniprot/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;RL18_ECOLI RL18_ECOLI&lt;/ins&gt;]] This is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;one of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteins that mediates the attachment of the 5S rRNA subcomplex onto the large &lt;/ins&gt;ribosomal subunit &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;where it forms part of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of &lt;/ins&gt;ribosome&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;-bound tRNAs.&amp;lt;ref&amp;gt;PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, &lt;/ins&gt;it &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly &lt;/ins&gt;to the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;5'-end of the 23S &lt;/ins&gt;rRNA&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates assembly &lt;/ins&gt;of the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S &lt;/ins&gt;subunit&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. It is not thought to be involved in the functions &lt;/ins&gt;of &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;the mature 50S subunit in vitro&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;proteins that surrounds the polypeptide exit tunnel on the outside of the subunit&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref&amp;gt;PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;3'-end of the 23S &lt;/ins&gt;rRNA&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, where it nucleates assembly of the 50S subunit&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This &lt;/ins&gt;protein &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;binds directly to at least 2 domains of the 23S ribosomal RNA, thus &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;important in its secondary structure. It is located near &lt;/ins&gt;the &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;subunit interface in the base of the L7/L12 stalk&lt;/ins&gt;, &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;and near the tRNA binding site of the peptidyltransferase center&lt;/ins&gt;.[HAMAP-Rule:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365&lt;/ins&gt;] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 18 Jul 2018 08:12:12 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 04:12, 5 August 2016</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=2640245&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 04:12, 5 August 2016&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{Large structure}}&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;StructureSection load='3j5l' size='340' side='right' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;StructureSection load='3j5l' size='340' side='right' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 5:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 6:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;], [http://pdbe.org/3j5l PDBe&lt;/ins&gt;], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5l ProSAT&lt;/ins&gt;]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/table&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{Large structure}}&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 17:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 19:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;From MEDLINE&amp;amp;reg;/PubMed&amp;amp;reg;, a database of the U.S. National Library of Medicine.&amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;From MEDLINE&amp;amp;reg;/PubMed&amp;amp;reg;, a database of the U.S. National Library of Medicine.&amp;lt;br&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/div&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/div&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div class=&amp;quot;pdbe-citations 3j5l&amp;quot; style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&amp;lt;/div&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== References ==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== References ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Fri, 05 Aug 2016 04:12:24 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 15:44, 25 December 2014</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=2282129&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 15:44, 25 December 2014&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{Large structure}}&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{STRUCTURE_3j5l|  PDB=3j5l  |  SCENE=  }} &lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;StructureSection load&lt;/ins&gt;=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'3j5l' size='340' side='right' caption='[[3j5l]], [[Resolution|resolution]] 6.60&amp;amp;Aring;' scene=''&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;=&lt;/del&gt;==Structure of the E. coli 50S subunit with ErmBL nascent chain===&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;== Structural highlights ==&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{ABSTRACT_PUBMED_24662426}}&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;table&amp;gt;&amp;lt;tr&amp;gt;&amp;lt;td colspan='2'&amp;gt;[[3j5l]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. For a &amp;lt;b&amp;gt;guided tour on the structure components&amp;lt;/b&amp;gt; use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J5L FirstGlance]. &amp;lt;br&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&amp;lt;tr id='ligand'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Ligand|Ligands:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=ERY:ERYTHROMYCIN+A'&amp;gt;ERY&amp;lt;/scene&amp;gt;, &amp;lt;scene name='pdbligand=UNL:UNKNOWN+LIGAND'&amp;gt;UNL&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Function==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;tr id='NonStdRes'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;[[Non-Standard_Residue|NonStd Res:]]&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'&amp;gt;MA6&amp;lt;/scene&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;tr id='resources'&amp;gt;&amp;lt;td class=&amp;quot;sblockLbl&amp;quot;&amp;gt;&amp;lt;b&amp;gt;Resources:&amp;lt;/b&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;td class=&amp;quot;sblockDat&amp;quot;&amp;gt;&amp;lt;span class='plainlinks'&amp;gt;[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j5l RCSB], [http://www.ebi.ac.uk/pdbsum/3j5l PDBsum]&amp;lt;/span&amp;gt;&amp;lt;/td&amp;gt;&amp;lt;/tr&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/table&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Function ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;  &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;div style=&amp;quot;background-color:#fffaf0;&amp;quot;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== Publication Abstract from PubMed ==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In bacteria, ribosome stalling during translation of ErmBL leader peptide occurs in the presence of the antibiotic erythromycin and leads to induction of expression of the downstream macrolide resistance methyltransferase ErmB. The lack of structures of drug-dependent stalled ribosome complexes (SRCs) has limited our mechanistic understanding of this regulatory process. Here we present a cryo-electron microscopy structure of the erythromycin-dependent ErmBL-SRC. The structure reveals that the antibiotic does not interact directly with ErmBL, but rather redirects the path of the peptide within the tunnel. Furthermore, we identify a key peptide-ribosome interaction that defines an important relay pathway from the ribosomal tunnel to the peptidyltransferase centre (PTC). The PTC of the ErmBL-SRC appears to adopt an uninduced state that prevents accommodation of Lys-tRNA at the A-site, thus providing structural basis for understanding how the drug and the nascent peptide cooperate to inhibit peptide bond formation and induce translation arrest.&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;==About this Structure==&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;,Arenz S, Ramu H, Gupta P, Berninghausen O, Beckmann R, Vazquez-Laslop N, Mankin AS, Wilson DN Nat Commun&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;2014 Mar 24;5&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;3501&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;doi: 10&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;1038&lt;/ins&gt;/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ncomms4501&lt;/ins&gt;. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;PMID&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;24662426&amp;lt;ref&amp;gt;PMID:24662426&amp;lt;&lt;/ins&gt;/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ref&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[3j5l]] is a 33 chain structure with sequence from [http://en&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;wikipedia&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org/wiki/Escherichia_coli Escherichia coli] and [http&lt;/del&gt;:&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;//en&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;wikipedia&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org&lt;/del&gt;/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;wiki/Streptococcus_sanguinis Streptococcus sanguinis]&lt;/del&gt;. &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Full crystallographic information is available from [http&lt;/del&gt;:/&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;/oca.weizmann.ac.il/oca-bin/ocashort?id=3J5L OCA]. &lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Reference&lt;/del&gt;==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;From MEDLINE&amp;amp;reg;/PubMed&amp;amp;reg;, a database of the U.S. National Library of Medicine.&amp;lt;br&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref group=&amp;quot;xtra&amp;quot;&amp;gt;PMID:024662426&amp;lt;/ref&amp;gt;&lt;/del&gt;&amp;lt;references &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;group=&amp;quot;xtra&amp;quot;&lt;/del&gt;/&amp;gt;&amp;lt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;references&lt;/del&gt;/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/div&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;== &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;References &lt;/ins&gt;==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;__TOC__&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;StructureSection&lt;/ins&gt;&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz, S&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Arenz, S]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Beckmann, R&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Beckmann, R]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Berninghausen, O&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Berninghausen, O]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Gupta, P&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Gupta, P]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Mankin, A S&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Mankin, A S]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ramu, H&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ramu, H]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Vazquez-Laslop, N&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Vazquez-Laslop, N]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Wilson, D N&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/del&gt;]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Wilson, D N]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Erythromycin]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Erythromycin]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ribosome-antibiotic complex]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Ribosome-antibiotic complex]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Stalling]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Stalling]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Thu, 25 Dec 2014 15:44:02 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 06:54, 2 April 2014</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=1908084&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 06:54, 2 April 2014&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 2:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 2:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{STRUCTURE_3j5l|  PDB=3j5l  |  SCENE=  }} &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{STRUCTURE_3j5l|  PDB=3j5l  |  SCENE=  }} &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;===Structure of the E. coli 50S subunit with ErmBL nascent chain===&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;===Structure of the E. coli 50S subunit with ErmBL nascent chain===&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{ABSTRACT_PUBMED_24662426}}&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Function==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Function==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 10:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 11:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Reference==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Reference==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references group=&amp;quot;xtra&amp;quot;/&amp;gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;ref group=&amp;quot;xtra&amp;quot;&amp;gt;PMID:024662426&amp;lt;/ref&amp;gt;&lt;/ins&gt;&amp;lt;references group=&amp;quot;xtra&amp;quot;/&amp;gt;&amp;lt;references/&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Escherichia coli]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Category: Streptococcus sanguinis]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 02 Apr 2014 06:54:41 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 09:28, 26 March 2014</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=1907046&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 09:28, 26 March 2014&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'''Unreleased &lt;/del&gt;structure&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'''&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{Large &lt;/ins&gt;structure&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;}}&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{STRUCTURE_3j5l|  PDB=3j5l  |  SCENE=  }} &lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;===Structure of the E. coli 50S subunit with ErmBL nascent chain===&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;entry 3j5l &lt;/del&gt;is &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ON HOLD &lt;/del&gt; &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;until Paper Publication&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;==Function==&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[http://www.uniprot.org/uniprot/RL29_ECOLI RL29_ECOLI]] Binds 23S rRNA. It is not essential for growth.[HAMAP-Rule:MF_00374]  One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI]] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B]  In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL16_ECOLI RL16_ECOLI]] This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_ECOLI RL21_ECOLI]] This protein binds to 23S rRNA in the presence of protein L20.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI]] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL17_ECOLI RL17_ECOLI]] Requires L15 for assembly into the 50S subunit.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL13_ECOLI RL13_ECOLI]] This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_01366] [[http://www.uniprot.org/uniprot/RL25_ECOLI RL25_ECOLI]] This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.[HAMAP-Rule:MF_01336] [[http://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI]] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.&amp;lt;ref&amp;gt;PMID:353728&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL4_ECOLI RL4_ECOLI]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Forms part of the polypeptide exit tunnel.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;   Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.&amp;lt;ref&amp;gt;PMID:2442760&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL9_ECOLI RL9_ECOLI]] One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.[HAMAP-Rule:MF_00503] [[http://www.uniprot.org/uniprot/RL24_ECOLI RL24_ECOLI]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;   One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.&amp;lt;ref&amp;gt;PMID:357435&amp;lt;/ref&amp;gt;  [[http://www.uniprot.org/uniprot/RL22_ECOLI RL22_ECOLI]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.[HAMAP-Rule:MF_01331_B]  The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL20_ECOLI RL20_ECOLI]] One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/RL23_ECOLI RL23_ECOLI]] One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL3_ECOLI RL3_ECOLI]] One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL5_ECOLI RL5_ECOLI]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.[HAMAP-Rule:MF_01333_B]  In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.[HAMAP-Rule:MF_01333_B]  Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL6_ECOLI RL6_ECOLI]] This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.[HAMAP-Rule:MF_01365]  Gentamicin-resistant mutations in this protein affect translation fidelity.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL15_ECOLI RL15_ECOLI]] This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL19_ECOLI RL19_ECOLI]] This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. &lt;/ins&gt;The &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;protein conformation &lt;/ins&gt;is &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;quite different between the 50S and 70S structures, which may be necessary for translocation.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL14_ECOLI RL14_ECOLI]] This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt;   Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.&amp;lt;ref&amp;gt;PMID:22829778&amp;lt;/ref&amp;gt; &lt;/ins&gt; &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Authors&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Arenz, S&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, Berninghausen, O&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, Beckmann, R&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, Wilson, D&lt;/del&gt;.&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;N&lt;/del&gt;.&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;==About this Structure==&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[3j5l]] is a 33 chain structure with sequence from [http&lt;/ins&gt;:&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;//en&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;wikipedia&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;ac&lt;/ins&gt;.&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;il/oca-bin/ocashort?id=3J5L OCA]&lt;/ins&gt;. &lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Description&lt;/del&gt;: &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Structure of the E. &lt;/del&gt;coli &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;50S subunit with ErmBL nascent chain&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;==Reference==&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;references group=&amp;quot;xtra&amp;quot;/&amp;gt;&amp;lt;references/&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category&lt;/ins&gt;: &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;Escherichia &lt;/ins&gt;coli&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Streptococcus sanguinis]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Arenz, S.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Beckmann, R.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Berninghausen, O.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Gupta, P.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Mankin, A S.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Ramu, H.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Vazquez-Laslop, N.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Wilson, D N.]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Erythromycin]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Ribosome-antibiotic complex]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;[[Category: Stalling]]&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 26 Mar 2014 09:28:36 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
		<item>
			<title>OCA at 07:02, 13 November 2013</title>
			<link>http://52.214.119.220/wiki/index.php?title=3j5l&amp;diff=1862671&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 07:02, 13 November 2013&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;'''Unreleased structure'''&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;'''Unreleased structure'''&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The entry 3j5l is ON HOLD &lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The entry 3j5l is ON HOLD &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; until Paper Publication&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Authors: Arenz S, Berninghausen O, Beckmann R, Wilson &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;DN&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Authors: Arenz&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/ins&gt;S&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/ins&gt;, Berninghausen&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/ins&gt;O&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/ins&gt;, Beckmann&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, &lt;/ins&gt;R&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;.&lt;/ins&gt;, Wilson&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;, D.N.&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Description: Structure of the E. coli 50S subunit with ErmBL nascent chain&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Description: Structure of the E. coli 50S subunit with ErmBL nascent chain&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Wed, 13 Nov 2013 07:02:17 GMT</pubDate>			<dc:creator>OCA</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:3j5l</comments>		</item>
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