Article
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains.
The EMBO journal - 15 Aug 2000
Prodromou C, Panaretou B, Chohan S, Siligardi G, O'Brien R, Ladbury J E, Roe S M, Piper P W, Pearl L H
Abstract excerpt
How the ATPase activity of Heat shock protein 90 (Hsp90) is coupled to client protein activation remains obscure. Using truncation and missense mutants of Hsp90, we analysed the structural implications of its ATPase cycle. C-terminal truncation mutants lacking inherent dimerization displayed reduced ATPase activity, but dimerized in the presence of 5'-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Adenylyl Imidodiphosphate
- Bacterial Proteins
- Circular Dichroism
- Cross-Linking Reagents
- DNA Gyrase
- DNA Topoisomerases, Type II
- Dimerization
- Escherichia coli Proteins