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Article

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes.

The Journal of biological chemistry - 18 Jun 1999

Grenert J P, Johnson B D, Toft D O

Abstract excerpt

The chaperone hsp90 is capable of binding and hydrolyzing ATP. Using information on a related ATPase, DNA gyrase B, we selected three conserved residues in hsp90's ATP-binding domain for mutation. Two of these mutations eliminate nucleotide binding, while the third retains nucleotide binding but...

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Identifiers

PMID: 10364185
DOI: 10.1074/jbc.274.25.17525

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-10364185-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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