<table><tr><td colspan='2'>[[2c7c]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2c7c]] is a 21 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=2C7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7C FirstGlance]. <br>
[[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] [[https://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
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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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==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]]
== References ==
== References ==
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Clare, D K]]
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[[Category: Clare DK]]
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[[Category: Farr, G W]]
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[[Category: Farr GW]]
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[[Category: Horwich, A L]]
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[[Category: Horwich AL]]
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[[Category: Houldershaw, D]]
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[[Category: Houldershaw D]]
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[[Category: Ranson, N A]]
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[[Category: Ranson NA]]
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[[Category: Saibil, H R]]
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[[Category: Saibil HR]]
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[[Category: Atomic structure fitting]]
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[[Category: Atp-binding]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Chaperone]]
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[[Category: Chaperonin]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphorylation]]
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Current revision
FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)
2c7c is a 21 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.,Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
