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Article

Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX.

The Journal of biological chemistry - 21 Oct 2005

Kang Sung Gyun, Dimitrova Mariana N, Ortega Joaquin, Ginsburg Ann, Maurizi Michael R

Abstract excerpt

The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a hollow-cored particle composed of two heptameric rings joined face-to-face forming an aqueous chamber containing the proteolytic active sites. We have found that isolated human mitochondrial ClpP (hClpP) is stable as a heptamer and remains a monodisperse species (s(20,w) 7.0 S; M(app) 169, 200) at concentrations > or = 3...

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PMID: 16115876
DOI: 10.1074/jbc.M507240200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX.PMID 16115876Read ↗

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