2c7c

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Revision as of 06:54, 21 November 2007

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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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