Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

Maruf M. U. Ali, S. Mark Roe, Cara K. Vaughan, Phillipe Meyer, Barry Panaretou, Peter W. Piper, Chrisostomos Prodromou and Laurence H. Pearl ()
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Maruf M. U. Ali: Institute of Cancer Research, Chester Beatty Laboratories
S. Mark Roe: Institute of Cancer Research, Chester Beatty Laboratories
Cara K. Vaughan: Institute of Cancer Research, Chester Beatty Laboratories
Phillipe Meyer: Institute of Cancer Research, Chester Beatty Laboratories
Barry Panaretou: King's College London
Peter W. Piper: The University of Sheffield
Chrisostomos Prodromou: Institute of Cancer Research, Chester Beatty Laboratories
Laurence H. Pearl: Institute of Cancer Research, Chester Beatty Laboratories

Nature, 2006, vol. 440, issue 7087, 1013-1017

Abstract: Abstract Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for the assembly and regulation of many eukaryotic signalling systems and is an emerging target for rational chemotherapy of many cancers. Although the structures of isolated domains of Hsp90 have been determined, the arrangement and ATP-dependent dynamics of these in the full Hsp90 dimer have been elusive and contentious. Here we present the crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1. The structure reveals the complex architecture of the ‘closed’ state of the Hsp90 chaperone, the extensive interactions between domains and between protein chains, the detailed conformational changes in the amino-terminal domain that accompany ATP binding, and the structural basis for stabilization of the closed state by p23/Sba1. Contrary to expectations, the closed Hsp90 would not enclose its client proteins but provides a bipartite binding surface whose formation and disruption are coupled to the chaperone ATPase cycle.

Date: 2006
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DOI: 10.1038/nature04716

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