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ATP‐driven molecular chaperone machines
Author(s) -
Clare Daniel K.,
Saibil Helen R.
Publication year - 2013
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22361
Subject(s) - groel , chaperonin , chaperone (clinical) , chemistry , protein folding , atp hydrolysis , molecular machine , hsp60 , co chaperone , atpase , hsp90 , biophysics , foldase , heat shock protein , folding (dsp implementation) , biochemistry , hsp70 , nanotechnology , enzyme , escherichia coli , biology , medicine , materials science , engineering , electrical engineering , gene , pathology
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. © 2013 The Authors. Published by Wiley Periodicals, Inc. Biopolymers 99: 846–859, 2013.