5w0s

<StructureSection load='5w0s' size='340' side='right' caption='[[5w0s]], [[Resolution|resolution]] 3.50&Aring;' scene=''>

<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>

</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>

[[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]

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.

 

== References ==

</StructureSection>

[[Category: Chiu, W]]

[[Category: Roh, S H]]

[[Category: Chaperone]]

[[Category: Conformational heterogeneity]]

[[Category: Groel]]