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Article

The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer.

The Journal of biological chemistry - 1 Apr 2005

Piszczek Grzegorz, Rozycki Jan, Singh Satyendra K, Ginsburg Ann, Maurizi Michael R

Abstract excerpt

Substrate recognition by Clp chaperones is dependent on interactions with motifs composed of specific peptide sequences. We studied the binding of short motif-bearing peptides to ClpA, the chaperone component of the ATP-dependent ClpAP protease of Escherichia coli in the presence of ATPgammaS and Mg2+ at pH 7.5. Binding was measured by isothermal titration calorimetry (ITC) using the peptide, AANDENYALAA, which...

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Source

Identifiers

PMID: 15657062
DOI: 10.1074/jbc.M411733200

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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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