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Article

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.

Molecular cell - 1 Mar 2003

Meyer Philippe, Prodromou Chrisostomos, Hu Bin, Vaughan Cara, Roe S Mark, Panaretou Barry, Piper Peter W, Pearl Laurence H

Abstract excerpt

Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains. The crystal structure of the middle segment of yeast Hsp90 reveals considerable evolutionary divergence from the equivalent regions of other GHKL protein family members such as MutL and GyrB, including an additional...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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PMID: 12667448
DOI: 10.1016/s1097-2765(03)00065-0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.PMID 12667448Read ↗

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains.Semantic proximity Read ↗

Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast.Semantic proximity Read ↗

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.Semantic proximity Read ↗

Evolution of the conformational dynamics of the molecular chaperone Hsp90.Semantic proximity Read ↗

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Semantic proximity Read ↗

Coordinated ATP hydrolysis by the Hsp90 dimer.Semantic proximity Read ↗

Mechanistic Asymmetry in Hsp90 Dimers.Semantic proximity Read ↗

A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket.Semantic proximity Read ↗

Functional and physical interaction between yeast Hsp90 and Hsp70.Semantic proximity Read ↗

N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.Semantic proximity Read ↗

Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Semantic proximity Read ↗

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.Semantic proximity Read ↗

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