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

Cited 82 time in WEB OF SCIENCE Cited 0 time in Scopus
Title
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
Author(s)
Kang, SG; Maurizi, MR; Thompson, M; Mueser, T; Ahvazi, B
KIOST Author(s)
Kang, Sung Gyun(강성균)
Publication Year
2004-12
Abstract
We have determined a 2.1 Angstrom 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 narrow (12 Angstrom) axial channel, positioned to interact with unfolded substrates translocated there by the associated ClpX chaperone. Mutation or deletion of these residues causes a drastic decrease in ClpX-mediated protein and peptide degradation. Residues 8-16 form a mobile loop that extends above the ring surface and is also required for activity. The 28 amino acid C-terminal domain, a unique feature of mammalian ClpP proteins, lies on the periphery of the ring, with its proximal portion forming a loop that extends out from the ring surface. Residues at the start of the C-terminal domain impinge on subunit interfaces within the ring and affect heptamer assembly and stability. We propose that the N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may play an important functional role as well. Published by Elsevier Inc.
ISSN
1047-8477
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/5183
DOI
10.1016/j.jsb.2004.07.004
Bibliographic Citation
JOURNAL OF STRUCTURAL BIOLOGY, v.148, no.3, pp.338 - 352, 2004
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Subject
ATP-DEPENDENT PROTEASE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; DEGRADATION; CHAPERONE; SEQUENCE; TRANSLOCATION; PROTEINS; SYMMETRY; PROGRAM
Keywords
mitochondrial ClpP; CIp/Hsp100; X-ray crystallography; ATP-dependent protease
Type
Article
Language
English
Document Type
Article
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
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