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Article

The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites.

Journal of molecular biology - 2 Mar 2001

Schlee S, Groemping Y, Herde P, Seidel R, Reinstein J

Abstract excerpt

ClpB belongs to the Hsp100 family and assists de-aggregation of protein aggregates by DnaK chaperone systems. It contains two Walker consensus sequences (or P-Loops) that indicate potential nucleotide binding domains (NBD). Both domains appear to be essential for chaperoning function, since mutation of the conserved lysine residue of the GX(4)GKT consensus sequences to glutamine (K204Q and K601Q) abolishes its...

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Share to Adenosine Diphosphate
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11243796
DOI: 10.1006/jmbi.2001.4455

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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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