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Article

Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.

Molecular cell - 6 Jul 2007

Martin Andreas, Baker Tania A, Sauer Robert T

Abstract excerpt

In the ClpXP proteolytic machine, ClpX uses the energy of ATP hydrolysis to unfold protein substrates and translocate them through a central pore and into the degradation chamber of ClpP. Here, we demonstrate a bipartite system of ClpX-ClpP interactions that serves multiple functional roles. High...

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Share to Adenosine Triphosphate
Share to ATPases Associated with Diverse Cellular Activities
Share to Endopeptidase Clp

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Molecular Chaperones

Share to Protein Processing, Post-Translational

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Source

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Identifiers

PMID: 17612489
DOI: 10.1016/j.molcel.2007.05.024
PMCID: PMC2074893

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17612489-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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