Crystal structure of the human mitochondrial chaperonin symmetrical football complex

Shahar Nisemblat, Oren Yaniv, Avital Parnas, Felix Frolow, Abdussalam Azem*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)6044-6049
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number19
StatePublished - 12 May 2015


FundersFunder number
European Synchrotron Radiation Facility
Israel Science Foundation1507/13, 1902/08


    • Chaperone
    • Hsp10
    • Hsp60
    • Mitochondrial chaperonin
    • Symmetrical complex


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