The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

Abstract

The molecular chaperone heat-shock protein 90 (Hsp90) is one of the most abundant proteins in unstressed eukaryotic cells. Its function is dependent on an exceptionally slow ATPase reaction that involves large conformational changes. To observe these conformational changes and to understand their interplay with the ATPase function, we developed a single… (More)
DOI: 10.1038/nsmb.1557

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@article{Mickler2009TheLC, title={The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis}, author={Moritz Mickler and Martin Hessling and Christoph Ratzke and Johannes Buchner and Thorsten Hugel}, journal={Nature Structural &Molecular Biology}, year={2009}, volume={16}, pages={281-286} }