1grl

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Current revision (07:26, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1grl' size='340' side='right'caption='[[1grl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1grl' size='340' side='right'caption='[[1grl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1grl]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1grl]] is a 7 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=1GRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRL FirstGlance]. <br>
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</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=1grl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grl OCA], [https://pdbe.org/1grl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1grl RCSB], [https://www.ebi.ac.uk/pdbsum/1grl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1grl ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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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=1grl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grl OCA], [https://pdbe.org/1grl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1grl RCSB], [https://www.ebi.ac.uk/pdbsum/1grl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1grl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
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[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1grl 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=1grl ConSurf].
<div style="clear:both"></div>
<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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The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.
 
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A.,Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB Nature. 1994 Oct 13;371(6498):578-86. PMID:7935790<ref>PMID:7935790</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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<div class="pdbe-citations 1grl" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boisvert, D C]]
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[[Category: Boisvert DC]]
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[[Category: Braig, K]]
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[[Category: Braig K]]
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[[Category: Hegde, R]]
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[[Category: Hegde R]]
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[[Category: Horwich, A L]]
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[[Category: Horwich AL]]
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[[Category: Joachimiak, A]]
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[[Category: Joachimiak A]]
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[[Category: Otwinowski, Z]]
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[[Category: Otwinowski Z]]
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[[Category: Sigler, P B]]
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[[Category: Sigler PB]]
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[[Category: Chaperonin]]
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Current revision

THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS

PDB ID 1grl

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