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Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis

19 Dec 2021

Abstract excerpt

ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self-compartmentalized peptidase. ClpXP is currently the only AAA+ protease for which high-resolution structures exist, the molecular basis of recognition for a protein substrate is understood, extensive biochemical and genetic analysis have been performed,...

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PMID: 34923891
DOI: 10.1080/10409238.2021.1979461

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Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysisPMID 34923891Read ↗

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 ↗

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinerySemantic proximity Read ↗

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

Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX.Semantic proximity Read ↗

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

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

A mitochondrial insertion directs substrate selection and engagement by ClpXSemantic proximity Read ↗

A conformational switch underlies ClpP protease function.Semantic proximity Read ↗

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Semantic proximity Read ↗

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