2j28

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[[Image:2j28.png|left|200px]]
 
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==MODEL OF E. COLI SRP BOUND TO 70S RNCS==
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The line below this paragraph, containing "STRUCTURE_2j28", creates the "Structure Box" on the page.
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<SX load='2j28' size='340' side='right' viewer='molstar' caption='[[2j28]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2j28]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J28 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2j28| PDB=2j28 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j28 OCA], [https://pdbe.org/2j28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j28 RCSB], [https://www.ebi.ac.uk/pdbsum/2j28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j28 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j2/2j28_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j28 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.
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===MODEL OF E. COLI SRP BOUND TO 70S RNCS===
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Following the signal sequence from ribosomal tunnel exit to signal recognition particle.,Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R Nature. 2006 Nov 23;444(7118):507-11. Epub 2006 Oct 29. PMID:17086193<ref>PMID:17086193</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17086193}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2j28" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17086193 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17086193}}
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==About this Structure==
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[[2j28]] is a 33 chain structure of [[Ribosomal protein L2]], [[Ribosomal protein L3]], [[Ribosomal protein L4]], [[Ribosomal protein L5]] and [[Ribosomal protein L6]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J28 OCA].
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==See Also==
==See Also==
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*[[Ribosomal protein L2]]
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*[[Ribosome 3D structures|Ribosome 3D structures]]
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*[[Ribosomal protein L3]]
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*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
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*[[Ribosomal protein L4]]
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== References ==
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*[[Ribosomal protein L5]]
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<references/>
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*[[Ribosomal protein L6]]
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__TOC__
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</SX>
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==Reference==
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<ref group="xtra">PMID:17086193</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Becker, T.]]
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[[Category: Large Structures]]
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[[Category: Beckmann, R.]]
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[[Category: Becker T]]
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[[Category: Blau, M.]]
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[[Category: Beckmann R]]
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[[Category: Halic, M.]]
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[[Category: Blau M]]
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[[Category: Mielke, T.]]
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[[Category: Halic M]]
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[[Category: Pool, M R.]]
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[[Category: Mielke T]]
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[[Category: Sinning, I.]]
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[[Category: Pool MR]]
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[[Category: Wild, K.]]
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[[Category: Sinning I]]
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[[Category: Protein-rna complex]]
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[[Category: Wild K]]
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[[Category: Ribosome]]
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[[Category: Signal recognition particle]]
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Current revision

MODEL OF E. COLI SRP BOUND TO 70S RNCS

2j28, resolution 8.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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