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Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):116-9. doi: 10.1107/S2053230X1303389X. Epub 2013 Dec 24.

Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins.

Author information

1
Department of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel.
2
The Daniella Rich Institute for Structural Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel.

Abstract

The mitochondrial Hsp60-Hsp10 complex assists the folding of various proteins impelled by ATP hydrolysis, similar to the bacterial chaperonins GroEL and GroES. The near-atomic structural details of the mitochondrial chaperonins are not known, despite the fact that almost two decades have passed since the structures of the bacterial chaperonins became available. Here, the crystallization procedure, diffraction experiments and structure determination by molecular replacement of the mammalian mitochondrial chaperonin HSP60 (E321K mutant) and its co-chaperonin Hsp10 are reported.

KEYWORDS:

mHsp10; mHsp60; mitochondrial chaperonins

PMID:
24419632
PMCID:
PMC3943094
DOI:
10.1107/S2053230X1303389X
[Indexed for MEDLINE]
Free PMC Article

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