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

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

Proteins - 1 Dec 2012

Zhang Ting, Ploetz Elizabeth A, Nagy Maria, Doyle Shannon M, Wickner Sue, Smith Paul E, Zolkiewski Michal

Abstract excerpt

ClpB reactivates aggregated proteins in cooperation with DnaK/J. The ClpB monomer contains two nucleotide-binding domains (D1, D2), a coiled-coil domain, and an N-terminal domain attached to D1 with a 17-residue-long unstructured linker containing a Gly-Gly motif. The ClpB-mediated protein disaggregation is linked to translocation of substrates through the central channel in the hexameric ClpB, but the events...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Endopeptidase Clp

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Glucosephosphate Dehydrogenase

Share to Heat-Shock Proteins

Share to Luciferases

Share to Molecular Dynamics Simulation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 22890624
DOI: 10.1002/prot.24159
PMCID: PMC3486956

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.PMID 22890624Read ↗

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

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

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

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

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

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

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

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

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

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

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