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

被引：0

作者：

Moritz Mickler

Martin Hessling

Christoph Ratzke

Johannes Buchner

Thorsten Hugel

机构：

[1] IMETUM,Physik

[2] CeNS,Department

[3] Department Chemie,undefined

[4] Center for Integrated Protein Science CIPSM,undefined

[5] Technische Universität München,undefined

来源：

Nature Structural & Molecular Biology | 2009年 / 16卷

关键词：

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中图分类号：

学科分类号：

摘要：

The Hsp90 chaperone is responsible for the stabilization of a large variety of regulatory proteins. Single-molecule FRET was used to examine the conformational dynamics of Hsp90 in its different nucleotide-bound states. The findings suggest that, in the absence of substrate and cochaperone proteins, Hsp90's conformational changes are not strongly coupled to ATP hydrolysis.

引用

页码：281 / 286

页数：5

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