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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 is apparently deficient in ATP hydrolysis. We first analyzed how these mutations affect hsp90's binding to the...

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Identifiers

PMID: 10364185
DOI: 10.1074/jbc.274.25.17525

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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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