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

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 mutat...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Allosteric Site
Share to Endopeptidase Clp

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP40 Heat-Shock Proteins

Share to ortho-Aminobenzoates

Share to Osmolar Concentration

Share to Protein Renaturation

Share to Thermus thermophilus

Source

Identifiers

PMID: 11243796
DOI: 10.1006/jmbi.2001.4455

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11243796-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites.PMID 11243796Read ↗

The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride.Semantic proximity Read ↗

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

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

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 ↗

Significance of Individual Domains of ClpL: A Novel Chaperone from Streptococcus mutans.Semantic proximity Read ↗

Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B.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 ↗

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

Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein.Semantic proximity Read ↗

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