5w0s: Difference between revisions

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==GroEL using cryoEM==
==GroEL using cryoEM==
<StructureSection load='5w0s' size='340' side='right' caption='[[5w0s]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<SX load='5w0s' size='340' side='right' viewer='molstar' caption='[[5w0s]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5w0s]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W0S FirstGlance]. <br>
<table><tr><td colspan='2'>[[5w0s]] is a 14 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=5W0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W0S FirstGlance]. <br>
</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=5w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w0s OCA], [http://pdbe.org/5w0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w0s RCSB], [http://www.ebi.ac.uk/pdbsum/5w0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w0s ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</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=5w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w0s OCA], [https://pdbe.org/5w0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w0s RCSB], [https://www.ebi.ac.uk/pdbsum/5w0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w0s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q6Q099_ECOLX Q6Q099_ECOLX]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600][RuleBase:RU000419]
[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]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Single-particle electron cryo-microscopy (cryo-EM) is an emerging tool for resolving structures of conformationally heterogeneous particles; however, each structure is derived from an average of many particles with presumed identical conformations. We used a 3.5-A cryo-EM reconstruction with imposed D7 symmetry to further analyze structural heterogeneity among chemically identical subunits in each GroEL oligomer. Focused classification of the 14 subunits in each oligomer revealed three dominant classes of subunit conformations. Each class resembled a distinct GroEL crystal structure in the Protein Data Bank. The conformational differences stem from the orientations of the apical domain. We mapped each conformation class to its subunit locations within each GroEL oligomer in our dataset. The spatial distributions of each conformation class differed among oligomers, and most oligomers contained 10-12 subunits of the three dominant conformation classes. Adjacent subunits were found to more likely assume the same conformation class, suggesting correlation among subunits in the oligomer. This study demonstrates the utility of cryo-EM in revealing structure dynamics within a single protein oligomer.


Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM.,Roh SH, Hryc CF, Jeong HH, Fei X, Jakana J, Lorimer GH, Chiu W Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):8259-8264. doi:, 10.1073/pnas.1704725114. Epub 2017 Jul 14. PMID:28710336<ref>PMID:28710336</ref>
==See Also==
 
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5w0s" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Chiu, W]]
[[Category: Escherichia coli]]
[[Category: Roh, S H]]
[[Category: Large Structures]]
[[Category: Chaperone]]
[[Category: Chiu W]]
[[Category: Conformational heterogeneity]]
[[Category: Roh SH]]
[[Category: Cryoem]]
[[Category: Groel]]

Latest revision as of 17:13, 13 March 2024

GroEL using cryoEMGroEL using cryoEM

5w0s, resolution 3.50Å

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