ATP-driven molecular chaperone machines

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

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.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Chaperonin 60 / chemistry
  • Escherichia coli* / metabolism
  • Molecular Chaperones* / chemistry
  • Protein Folding

Substances

  • Chaperonin 60
  • Molecular Chaperones
  • Adenosine Triphosphate