2c7c
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7c OCA], [http://www.ebi.ac.uk/pdbsum/2c7c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c7c RCSB]</span> | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:25 2008'' |
Revision as of 23:17, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)
Overview
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.
About this Structure
2C7C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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