期刊
BIOPOLYMERS
卷 99, 期 11, 页码 846-859出版社
WILEY
DOI: 10.1002/bip.22361
关键词
chaperones; machines; ATP driven; GroEL; Cryo-EM
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. (c) 2013 Wiley Periodicals, Inc. Biopolymers 99: 846-859, 2013.
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