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Article

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

Journal of structural biology - 1 Dec 2004

Kang Sung Gyun, Maurizi Michael R, Thompson Mark, Mueser Timothy, Ahvazi Bijan

Abstract excerpt

We have determined a 2.1 A crystal structure for human mitochondrial ClpP (hClpP), the proteolytic component of the ATP-dependent ClpXP protease. HClpP has a structure similar to that of the bacterial enzyme, with the proteolytic active sites sequestered within an aqueous chamber formed by face-to-face assembly of the two heptameric rings. The hydrophobic N-terminal peptides of the subunits are bound within the...

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Identifiers

PMID: 15522782
DOI: 10.1016/j.jsb.2004.07.004

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.PMID 15522782Read ↗

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