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Article

Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine.

Cell reports - 11 Aug 2015

Iosefson Ohad, Olivares Adrian O, Baker Tania A, Sauer Robert T

Abstract excerpt

In the axial channels of ClpX and related hexameric AAA+ protein-remodeling rings, the pore-1 loops are thought to play important roles in engaging, mechanically unfolding, and translocating protein substrates. How these loops perform these functions and whether they also prevent substrate dissociation to ensure processive degradation by AAA+ proteases are open questions. Using ClpX pore-1-loop variants,...

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Identifiers

PMID: 26235618
DOI: 10.1016/j.celrep.2015.07.007
PMCID: PMC4536184

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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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Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine.PMID 26235618Read ↗

Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine.Semantic proximity Read ↗

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

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

Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.Semantic proximity Read ↗

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysisSemantic proximity Read ↗

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

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.Semantic proximity Read ↗

Dynamic structural states of ClpB involved in its disaggregation function.Semantic proximity Read ↗

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