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Biopolymers. 2013 Nov;99(11):846-59. doi: 10.1002/bip.22361.

ATP-driven molecular chaperone machines.

Author information

1
Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.

Abstract

This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail. Cryo-electron microscopy analysis of the E. coli Hsp60 GroEL reveals intermediate conformations in the ATPase cycle and in substrate folding. These structures suggest a mechanism by which GroEL can forcefully unfold and then encapsulate substrates for subsequent folding in isolation from all other binding surfaces.

KEYWORDS:

ATP driven; Cryo-EM; GroEL; chaperones; machines

PMID:
23877967
PMCID:
PMC3814418
DOI:
10.1002/bip.22361
[Indexed for MEDLINE]
Free PMC Article

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