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Article

Coordinated ATP hydrolysis by the Hsp90 dimer.

The Journal of biological chemistry - 7 Sept 2001

Richter K, Muschler P, Hainzl O, Buchner J

Abstract excerpt

The Hsp90 dimer is a molecular chaperone with an unusual N-terminal ATP binding site. The structure of the ATP binding site makes it a member of a new class of ATP-hydrolyzing enzymes, known as the GHKL family. While for some of the family members structural data on conformational changes occurring after ATP binding are available, these are still lacking for Hsp90. Here we set out to investigate the correlation...

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Identifiers

PMID: 11441008
DOI: 10.1074/jbc.M103832200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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