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Article

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

Nature structural & molecular biology - 6 May 2012

Glynn Steven E, Nager Andrew R, Baker Tania A, Sauer Robert T

Abstract excerpt

In the Escherichia coli ClpXP protease, a hexameric ClpX ring couples ATP binding and hydrolysis to mechanical protein unfolding and translocation into the ClpP degradation chamber. Rigid-body packing between the small AAA+ domain of each ClpX subunit and the large AAA+ domain of its neighbor stabilizes the hexamer. By connecting the parts of each rigid-body unit with disulfide bonds or linkers, we created...

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Share to ATPases Associated with Diverse Cellular Activities
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22562135
DOI: 10.1038/nsmb.2288
PMCID: PMC3372766

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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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