ATP-driven molecular chaperone machines.
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ABSTRACT:
SUBMITTER: Clare DK
PROVIDER: S-EPMC3814418 | biostudies-literature | 2013 Nov
REPOSITORIES: biostudies-literature
Publications
ATP-driven molecular chaperone machines.
Clare Daniel K DK Saibil Helen R HR
Biopolymers 20131101 11
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 mechanis ...[more]
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