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Article

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.

Journal of molecular biology - 28 Jul 1995

Kessel M, Maurizi M R, Kim B, Kocsis E, Trus B L, Singh S K, Steven A C

Abstract excerpt

Energy-dependent protein degradation is carried out by large multimeric protein complexes such as the proteasomes of eukaryotic and archaeal cells and the ATP-dependent proteases of eubacterial cells. Clp protease, a major multicomponent protease of Escherichia coli, consists of a proteolytic component, ClpP, in association with an ATP-hydrolyzing, chaperonin-like component, ClpA. To provide a structural basis...

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Identifiers

PMID: 7623377
DOI: 10.1006/jmbi.1995.0400

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.PMID 7623377Read ↗

Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins.Semantic proximity Read ↗

The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes.Semantic proximity Read ↗

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.Semantic proximity Read ↗

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.Semantic proximity Read ↗

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

The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.Semantic proximity Read ↗

Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly.Semantic proximity Read ↗

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

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

Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadSemantic proximity Read ↗

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

Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.Semantic proximity Read ↗

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