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Article

Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli.

Journal of molecular biology - 10 Nov 2000

Kim K I, Cheong G W, Park S C, Ha J S, Woo K M, Choi S J, Chung C H

Abstract excerpt

The heat-shock protein ClpB is a protein-activated ATPase that is essential for survival of Escherichia coli at high temperatures. ClpB has also recently been suggested to function as a chaperone in reactivation of aggregated proteins. In addition, the clpB gene has been shown to contain two translational initiation sites and therefore encode two polypeptides of different size. To determine the structural...

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Identifiers

PMID: 11061966
DOI: 10.1006/jmbi.2000.4165

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli.PMID 11061966Read ↗

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Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Semantic proximity Read ↗

Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.Semantic proximity Read ↗

ClpB is the Escherichia coli heat shock protein F84.1.Semantic proximity Read ↗

The amino-terminal domain of ClpB supports binding to strongly aggregated proteins.Semantic proximity Read ↗

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.Semantic proximity Read ↗

Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.Semantic proximity Read ↗

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

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