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Article

Characterization of a trap mutant of the AAA+ chaperone ClpB.

The Journal of biological chemistry - 29 Aug 2003

Weibezahn Jimena, Schlieker Christian, Bukau Bernd, Mogk Axel

Abstract excerpt

The AAA+ protein ClpB mediates the solubilization of protein aggregates in cooperation with the DnaK chaperone system (KJE). The order of action of ClpB and KJE on aggregated proteins is unknown. We describe a ClpB variant with mutational alterations in the Walker B motif of both AAA domains (E279A/E678A), which binds but does not hydrolyze ATP. This variant associates in vitro and in vivo in a stable manner with...

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Identifiers

PMID: 12805357
DOI: 10.1074/jbc.M303653200

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a trap mutant of the AAA+ chaperone ClpB.PMID 12805357Read ↗

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Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Semantic proximity Read ↗

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling 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 ↗

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

Structural and Functional Insights into the Action Mode of A Mitochondrial AAA+ Disaggregase CLPBSemantic proximity Read ↗

ClpB chaperone passively threads soluble denatured proteins through its central pore.Semantic proximity Read ↗

Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization.Semantic proximity Read ↗

Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.Semantic proximity Read ↗

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

A tightly regulated molecular toggle controls AAA+ disaggregase.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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