{"doi":"10.1002/bip.22361","title":"ATP‐driven molecular chaperone machines","abstract":"<jats:title>ABSTRACT</jats:title><jats:p>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 <jats:italic>E. coli</jats:italic> 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. 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