TY  - JOUR
A1  - Hahn, Alexander
A1  - Parey, Kristian
A1  - Bublitz, Maike
A1  - Mills, Deryck J.
A1  - Zickermann, Volker
A1  - Vonck, Janet
A1  - Kühlbrandt, Werner
A1  - Meier, Thomas Kurt
T1  - Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
T2  - Molecular cell
N2  - Highlights
• Cryo-EM structure of a yeast F1Fo-ATP synthase dimer
• Inhibitor-free X-ray structure of the F1 head and rotor complex
• Mechanism of ATP generation by rotary catalysis
• Structural basis of cristae formation in the inner mitochondrial membrane
Summary
We determined the structure of a complete, dimeric F1Fo-ATP synthase from yeast Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The final structure resolves 58 of the 60 dimer subunits. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Subunit 8 (A6L in human) is an evolutionary derivative of the bacterial b subunit. On the lumenal membrane surface, subunit f establishes direct contact between the two monomers. Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e and g at the lateral dimer interface. They do not form dimer contacts but enable dimer formation by inducing.
KW  - mitochondria
KW  - inner membrane morphology
KW  - FF-ATP synthase dimer
KW  - bioenergetics
KW  - membrane protein complex
KW  - rotary ATPase mechanism
KW  - yeast
KW  - cryoelectron microscopy
KW  - X-ray crystallography
Y1  - 2016
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/77225
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-772258
SN  - 1097-2765
VL  - 63
IS  - 3
SP  - 445
EP  - 456
PB  - Elsevier
CY  - Amsterdam
ER  -