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Proc Natl Acad Sci U S A. 2015 May 12;112(19):6044-9. doi: 10.1073/pnas.1411718112. Epub 2015 Apr 27.

Crystal structure of the human mitochondrial chaperonin symmetrical football complex.

Author information

1
Departments of Biochemistry and Molecular Biology and The Daniella Rich Institute for Structural Biology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
2
The Daniella Rich Institute for Structural Biology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel Molecular Microbiology and Biotechnology, and.
3
Departments of Biochemistry and Molecular Biology and The Daniella Rich Institute for Structural Biology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel azema@tauex.tau.ac.il.

Abstract

Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a football-shaped, double-ring human mitochondrial chaperonin complex at 3.15 Å, which is a novel intermediate, likely representing the complex in an early stage of dissociation. Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit asymmetry within the rings and nucleotide symmetry between the rings. Moreover, the chaperonin tetradecamers show a different interring subunit arrangement when compared to GroEL. Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the mechanism of the well-studied Escherichia coli system.

KEYWORDS:

Hsp10; Hsp60; chaperone; mitochondrial chaperonin; symmetrical complex

PMID:
25918392
PMCID:
PMC4434751
DOI:
10.1073/pnas.1411718112
[Indexed for MEDLINE]
Free PMC Article

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