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Article

Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity.

Journal of molecular biology - 2 Aug 2002

Liu Zhonghua, Tek Vekalet, Akoev Vladimir, Zolkiewski Michal

Abstract excerpt

ClpB from Escherichia coli is a member of a protein-disaggregating multi-chaperone system that also includes DnaK, DnaJ, and GrpE. The sequence of ClpB contains two ATP-binding domains that are enclosed between the amino-terminal and carboxyl-terminal regions. The N-terminal sequence region does not contain known functional sequence motifs. Here, we performed site-directed mutagenesis of four polar residues...

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Identifiers

PMID: 12139937
DOI: 10.1016/s0022-2836(02)00591-0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity.PMID 12139937Read ↗

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