Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Biochemical journal - 12 Jun 2009

Watanabe Yo-Hei, Nakazaki Yosuke, Suno Ryoji, Yoshida Masasuke

Abstract excerpt

The ClpB chaperone forms a hexamer ring and rescues aggregated proteins in co-operation with the DnaK system. Each subunit of ClpB has two nucleotide-binding modules, AAA (ATPase associated with various cellular activities)-1 and AAA-2, and an 85-A (1 A=0.1 nm)-long coiled-coil. The coiled-coil consists of two halves: wing-1, leaning toward AAA-1, and wing-2, leaning away from all the domains. The coiled-coil is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Caseins
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Molecular Chaperones

Share to Protein Conformation

Share to Protein Denaturation

Share to Protein Subunits

Share to Thermus thermophilus

Source

Identifiers

PMID: 19351326
DOI: 10.1042/BJ20082238

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.PMID 19351326Read ↗

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 ↗

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

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

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

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

Characterization of a trap mutant of the AAA+ chaperone ClpB.Semantic proximity Read ↗

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

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

Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity.Semantic proximity Read ↗

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

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

⌁Select a neighboring publication to make it the new centre.