Apo‐Hsp90 coexists in two open conformational states in solution
Biology of the Cell2008Vol. 100(7), pp. 413–425
Citations Over TimeTop 10% of 2008 papers
Patrick Bron, Emmanuel Giudice, Jean‐Paul Rolland, Rubén M. Buey, Pascale Barbier, J. Fernando Dı́az, Vincent Peyrot, Daniel Thomas, Cyrille Garnier
Abstract
The present study shows, for the first time, the structure of the entire eukaryotic apo-Hsp90, along with its intrinsic flexibility. Although large structural rearrangements, leading to partial closure of the Hsp90 dimer, were previously attributed to the binding of nucleotides, our results reveal that they are in fact mainly due to the intrinsic flexibility of Hsp90 dimer. Taking into account the preponderant role of the dynamic nature of the structure of Hsp90, we reconsider the Hsp90 ATPase cycle.
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