Journal
MOLECULAR CELL
Volume 63, Issue 3, Pages 445-456Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2016.05.037
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Funding
- Max-Planck Society
- Collaborative Research Center of the German Research Foundation (DFG) [(SFB) 807]
- Cluster of Excellence Frankfurt Macromolecular Complexes (DFG) [EXC 115]
- Wellcome Trust [WT110068/Z/15/Z]
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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 F-o 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 a strong membrane curvature of similar to 100 degrees. Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.
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