1jzx - Revision history

OCA at 07:43, 7 February 2024

2024-02-07T07:43:04Z

←Older revision		Revision as of 07:43, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='1jzx' size='340' side='right'caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='1jzx' size='340' side='right'caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from ~~[https://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and~~ [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.1Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=Y:~~2-DEOXY-N6-(S)STYRENE+OXIDE+ADENOSINE+MONOPHOSPHATE~~'>Y</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;~~'>~~[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]~~</~~div~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [https://pdbe.org/1jzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [https://www.ebi.ac.uk/pdbsum/1jzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzx ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [https://pdbe.org/1jzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [https://www.ebi.ac.uk/pdbsum/1jzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RL32_DEIRA RL32_DEIRA]] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [[https://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [[https://www.uniprot.org/uniprot/RL4_DEIRA RL4_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B]	+	[https://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA] 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 (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</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=1jzx ConSurf].		</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=1jzx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we determined the high-resolution X-ray structures of the 50S ribosomal subunit of the eubacterium Deinococcus radiodurans, complexed with the clinically relevant antibiotics chloramphenicol, clindamycin and the three macrolides erythromycin, clarithromycin and roxithromycin. We found that antibiotic binding sites are composed exclusively of segments of 23S ribosomal RNA at the peptidyl transferase cavity and do not involve any interaction of the drugs with ribosomal proteins. Here we report the details of antibiotic interactions with the components of their binding sites. Our results also show the importance of putative Mg+2 ions for the binding of some drugs. This structural analysis should facilitate rational drug design.
-
-	Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria.,Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599<ref>PMID:11677599</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 25:
	*[[Ribosomal protein L32\|Ribosomal protein L32]]		*[[Ribosomal protein L32\|Ribosomal protein L32]]
	*[[Ribosomal protein L4\|Ribosomal protein L4]]		*[[Ribosomal protein L4\|Ribosomal protein L4]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Micrococcus radiodurans raj et al. 1960]]
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Albrecht, R]]	+	[[Category: Albrecht R]]
-	[[Category: Bashan, A]]	+	[[Category: Bashan A]]
-	[[Category: Franceschi, F]]	+	[[Category: Franceschi F]]
-	[[Category: Harms, J]]	+	[[Category: Harms J]]
-	[[Category: Schluenzen, F]]	+	[[Category: Schluenzen F]]
-	[[Category: Tocilj, A]]	+	[[Category: Tocilj A]]
-	[[Category: Yonath, A]]	+	[[Category: Yonath A]]
-	[[Category: Zarivach, R]]	+	[[Category: Zarivach R]]
-	~~[[Category: Antibiotic]]~~	+
-	~~[[Category: Clindamycin]]~~	+
-	~~[[Category: Peptidyl transferase center]]~~	+
-	~~[[Category: Ribosome~~]]	+

OCA at 08:44, 21 April 2021

2021-04-21T08:44:25Z

←Older revision		Revision as of 08:44, 21 April 2021
Line 3:		Line 3:
	<StructureSection load='1jzx' size='340' side='right'caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='1jzx' size='340' side='right'caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and [~~http~~://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1JZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Y:2-DEOXY-N6-(S)STYRENE+OXIDE+ADENOSINE+MONOPHOSPHATE'>Y</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Y:2-DEOXY-N6-(S)STYRENE+OXIDE+ADENOSINE+MONOPHOSPHATE'>Y</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [~~http~~://pdbe.org/1jzx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1jzx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzx ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [https://pdbe.org/1jzx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [https://www.ebi.ac.uk/pdbsum/1jzx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RL32_DEIRA RL32_DEIRA]] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [[~~http~~://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [[~~http~~://www.uniprot.org/uniprot/RL4_DEIRA RL4_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B]	+	[[https://www.uniprot.org/uniprot/RL32_DEIRA RL32_DEIRA]] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [[https://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [[https://www.uniprot.org/uniprot/RL4_DEIRA RL4_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:38, 17 July 2019

2019-07-17T13:38:28Z

←Older revision		Revision as of 13:38, 17 July 2019
Line 1:		Line 1:

	==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==		==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==
-	<StructureSection load='1jzx' size='340' side='right' caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>	+	<StructureSection load='1jzx' size='340' side='right'caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzx_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ribosomal protein L22\|Ribosomal protein L22]]
		+	*[[Ribosomal protein L32\|Ribosomal protein L32]]
		+	*[[Ribosomal protein L4\|Ribosomal protein L4]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 41:
	[[Category: Micrococcus radiodurans raj et al. 1960]]		[[Category: Micrococcus radiodurans raj et al. 1960]]
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
		+	[[Category: Large Structures]]
	[[Category: Albrecht, R]]		[[Category: Albrecht, R]]
	[[Category: Bashan, A]]		[[Category: Bashan, A]]
Line 44:		Line 50:
	[[Category: Yonath, A]]		[[Category: Yonath, A]]
	[[Category: Zarivach, R]]		[[Category: Zarivach, R]]
-	[[Category: 5]]
	[[Category: Antibiotic]]		[[Category: Antibiotic]]
	[[Category: Clindamycin]]		[[Category: Clindamycin]]
	[[Category: Peptidyl transferase center]]		[[Category: Peptidyl transferase center]]
	[[Category: Ribosome]]		[[Category: Ribosome]]

OCA at 07:27, 11 October 2017

2017-10-11T07:27:28Z

←Older revision		Revision as of 07:27, 11 October 2017
Line 1:		Line 1:
		+
	==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==		==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==
	<StructureSection load='1jzx' size='340' side='right' caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='1jzx' size='340' side='right' caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960] and [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Y:2-DEOXY-N6-(S)STYRENE+OXIDE+ADENOSINE+MONOPHOSPHATE'>Y</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://pdbe.org/1jzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://pdbe.org/1jzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1jzx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Ribosomal protein L22\|Ribosomal protein L22]]
-	*[[Ribosomal protein L32\|Ribosomal protein L32]]
-	*[[Ribosomal protein L4\|Ribosomal protein L4]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Micrococcus radiodurans raj et al. 1960]]
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
	[[Category: Albrecht, R]]		[[Category: Albrecht, R]]

OCA at 16:22, 11 September 2015

2015-09-11T16:22:59Z

←Older revision		Revision as of 16:22, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://pdbe.org/1jzx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1jzx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ribosomal protein L22\|Ribosomal protein L22]]
		+	*[[Ribosomal protein L32\|Ribosomal protein L32]]
		+	*[[Ribosomal protein L4\|Ribosomal protein L4]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:57, 25 December 2014

2014-12-25T18:57:14Z

←Older revision		Revision as of 18:57, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RL32_DEIRA RL32_DEIRA]] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [[http://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL4_DEIRA RL4_DEIRA]] 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 (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
-	[[Category: Albrecht, R.]]	+	[[Category: Albrecht, R]]
-	[[Category: Bashan, A.]]	+	[[Category: Bashan, A]]
-	[[Category: Franceschi, F.]]	+	[[Category: Franceschi, F]]
-	[[Category: Harms, J.]]	+	[[Category: Harms, J]]
-	[[Category: Schluenzen, F.]]	+	[[Category: Schluenzen, F]]
-	[[Category: Tocilj, A.]]	+	[[Category: Tocilj, A]]
-	[[Category: Yonath, A.]]	+	[[Category: Yonath, A]]
-	[[Category: Zarivach, R~~.]]~~	+	[[Category: Zarivach, R]]
-	~~[[Category: 23]]~~	+
-	~~[[Category: 50~~]]	+
	[[Category: 5]]		[[Category: 5]]
	[[Category: Antibiotic]]		[[Category: Antibiotic]]

OCA at 14:34, 28 September 2014

2014-09-28T14:34:21Z

←Older revision		Revision as of 14:34, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1jzx.~~png~~\|~~left~~\|200px]]	+	==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==
		+	<StructureSection load='1jzx' size='340' side='right' caption='[[1jzx]], [[Resolution\|resolution]] 3.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JZX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLY:CLINDAMYCIN'>CLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jzy\|1jzy]], [[1jzz\|1jzz]], [[1k00\|1k00]], [[1k01\|1k01]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jzx RCSB], [http://www.ebi.ac.uk/pdbsum/1jzx PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzx_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we determined the high-resolution X-ray structures of the 50S ribosomal subunit of the eubacterium Deinococcus radiodurans, complexed with the clinically relevant antibiotics chloramphenicol, clindamycin and the three macrolides erythromycin, clarithromycin and roxithromycin. We found that antibiotic binding sites are composed exclusively of segments of 23S ribosomal RNA at the peptidyl transferase cavity and do not involve any interaction of the drugs with ribosomal proteins. Here we report the details of antibiotic interactions with the components of their binding sites. Our results also show the importance of putative Mg+2 ions for the binding of some drugs. This structural analysis should facilitate rational drug design.

-	~~{{STRUCTURE_1jzx\| PDB=1jzx \| SCENE= }}~~	+	Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria.,Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599<ref>PMID:11677599</ref>

-	~~===Structural Basis for the Interaction~~ of ~~Antibiotics with~~ the ~~Peptidyl Transferase Center in Eubacteria===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11677599}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1jzx]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA].~~	+	</StructureSection>
-		+
-	==~~See Also==~~	+
-	*[[Ribosomal protein L22\|Ribosomal protein L22]]	+
-	*[[Ribosomal protein L32\|Ribosomal protein L32]]	+
-	*[[Ribosomal protein L4\|Ribosomal protein L4]]	+
-		+
-	~~==Reference~~==	+
-	<~~ref group="xtra">PMID:011677599<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
	[[Category: Albrecht, R.]]		[[Category: Albrecht, R.]]

OCA at 20:15, 20 October 2012

2012-10-20T20:15:27Z

←Older revision		Revision as of 20:15, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1jzx]] is a 4 chain structure ~~of [[Ribosomal protein L22]], [[Ribosomal protein L32]] and [[Ribosomal protein L4]]~~ with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA].	+	[[1jzx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA].

	==See Also==		==See Also==

OCA: Protected "1jzx" [edit=sysop:move=sysop]

2012-07-27T09:54:30Z

Protected "1jzx" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:54, 27 July 2012

OCA at 09:54, 27 July 2012

2012-07-27T09:54:29Z

←Older revision		Revision as of 09:54, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1jzx.png\|left\|200px]]		[[Image:1jzx.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1jzx", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1jzx\| PDB=1jzx \| SCENE= }}		{{STRUCTURE_1jzx\| PDB=1jzx \| SCENE= }}

	===Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria===		===Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11677599}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11677599 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_11677599}}		{{ABSTRACT_PUBMED_11677599}}

	==About this Structure==		==About this Structure==
-	~~1JZX~~ is a 4 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA].	+	[[1jzx]] is a 4 chain structure of [[Ribosomal protein L22]], [[Ribosomal protein L32]] and [[Ribosomal protein L4]] with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZX OCA].
		+
		+	==See Also==
		+	*[[Ribosomal protein L22\|Ribosomal protein L22]]
		+	*[[Ribosomal protein L32\|Ribosomal protein L32]]
		+	*[[Ribosomal protein L4\|Ribosomal protein L4]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11677599~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011677599</ref><references group="xtra"/>
	[[Category: Deinococcus radiodurans]]		[[Category: Deinococcus radiodurans]]
	[[Category: Albrecht, R.]]		[[Category: Albrecht, R.]]
Line 40:		Line 33:
	[[Category: Peptidyl transferase center]]		[[Category: Peptidyl transferase center]]
	[[Category: Ribosome]]		[[Category: Ribosome]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 03:40:23 2009''