TY - JOUR
T1 - Crystal structure of the human mitochondrial chaperonin symmetrical football complex
AU - Nisemblat, Shahar
AU - Yaniv, Oren
AU - Parnas, Avital
AU - Frolow, Felix
AU - Azem, Abdussalam
PY - 2015/5/12
Y1 - 2015/5/12
N2 - 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.
AB - 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.
KW - Chaperone
KW - Hsp10
KW - Hsp60
KW - Mitochondrial chaperonin
KW - Symmetrical complex
UR - http://www.scopus.com/inward/record.url?scp=84929192719&partnerID=8YFLogxK
U2 - 10.1073/pnas.1411718112
DO - 10.1073/pnas.1411718112
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AN - SCOPUS:84929192719
SN - 0027-8424
VL - 112
SP - 6044
EP - 6049
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 19
ER -