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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.

ABSTRACT: 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.

SUBMITTER: Ranson NA

PROVIDER: S-EPMC2871290 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.

Ranson Neil A NA Clare Daniel K DK Farr George W GW Houldershaw David D Horwich Arthur L AL Saibil Helen R HR

Nature structural & molecular biology 20060122 2

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. A ...[more]

PMID: 16429154

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