Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 19, Pages 6044-6049Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1411718112
Keywords
mitochondrial chaperonin; symmetrical complex; Hsp60; chaperone; Hsp10
Categories
Funding
- Israel Ministry of Science
- Legacy Heritage Biomedical Program of the Israel Science Foundation [1902/08]
- Israel Science Foundation [1507/13]
Ask authors/readers for more resources
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 angstrom, 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available