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Article

Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB.

Journal of molecular biology - 18 Apr 2008

Werbeck Nicolas D, Schlee Sandra, Reinstein Jochen

Abstract excerpt

The bacterial AAA+ protein ClpB and its eukaryotic homologue Hsp104 ensure thermotolerance of their respective organisms by reactivating aggregated proteins in cooperation with the Hsp70/Hsp40 chaperone system. Like many members of the AAA+ superfamily, the ClpB protomers form ringlike homohexameric complexes. The mechanical energy necessary to disentangle protein aggregates is provided by ATP hydrolysis at the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 18343405
DOI: 10.1016/j.jmb.2008.02.026

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB.PMID 18343405Read ↗

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 ↗

trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.Semantic proximity Read ↗

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Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.Semantic proximity Read ↗

Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.Semantic proximity Read ↗

Dynamic structural states of ClpB involved in its disaggregation function.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 ↗

A tightly regulated molecular toggle controls AAA+ disaggregase.Semantic proximity Read ↗

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Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein.Semantic proximity Read ↗

ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2.Semantic proximity Read ↗

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.Semantic proximity Read ↗

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