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Article

Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease.

Proceedings of the National Academy of Sciences of the United States of America - 13 Oct 2020

Zuromski Kristin L, Sauer Robert T, Baker Tania A

Abstract excerpt

ClpA is a hexameric double-ring AAA+ unfoldase/translocase that functions with the ClpP peptidase to degrade proteins that are damaged or unneeded. How the 12 ATPase active sites of ClpA, 6 in the D1 ring and 6 in the D2 ring, work together to fuel ATP-dependent degradation is not understood. We use site-specific cross-linking to engineer ClpA hexamers with alternating ATPase-active and ATPase-inactive modules in...

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Identifiers

PMID: 33020301
DOI: 10.1073/pnas.2014407117
PMCID: PMC7568338

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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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