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Article

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.

Nature structural & molecular biology - 1 Nov 2008

Martin Andreas, Baker Tania A, Sauer Robert T

Abstract excerpt

Proteolytic AAA+ unfoldases use ATP hydrolysis to power conformational changes that mechanically denature protein substrates and then translocate the polypeptide through a narrow pore into a degradation chamber. We show that a tyrosine residue in a pore loop of the hexameric ClpX unfoldase links ATP hydrolysis to mechanical work by gripping substrates during unfolding and translocation. Removal of the aromatic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 18931677
DOI: 10.1038/nsmb.1503
PMCID: PMC2610342

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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.

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