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Crystallization and structure determination of a symmetrical `football' complex of the mammalian mitochondrial Hsp60–Hsp10 chaperonins
Author(s) -
Nisemblat Shahar,
Parnas Avital,
Yaniv Oren,
Azem Abdussalam,
Frolow Felix
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1303389x
Subject(s) - chaperonin , hsp60 , crystallization , biology , physics , microbiology and biotechnology , heat shock protein , genetics , thermodynamics , hsp70 , protein folding , gene
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.