Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.
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ABSTRACT:
SUBMITTER: Lopez A
PROVIDER: S-EPMC8682993 | biostudies-literature | 2021 Dec
REPOSITORIES: biostudies-literature
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Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.
Lopez Abraham A Dahiya Vinay V Delhommel Florent F Freiburger Lee L Stehle Ralf R Asami Sam S Rutz Daniel D Blair Laura L Buchner Johannes J Sattler Michael M
Science advances 20211217 51
Hsp90 is a molecular chaperone that interacts with a specific set of client proteins and assists their folding. The underlying molecular mechanisms, involving dynamic transitions between open and closed conformations, are still enigmatic. Combining nuclear magnetic resonance, small-angle x-ray scattering, and biochemical experiments, we have identified a key intermediate state of Hsp90 induced by adenosine triphosphate (ATP) binding, in which rotation of the Hsp90 N-terminal domain (NTD) yields ...[more]
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