Title | Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. |
Publication Type | Journal Article |
Year of Publication | 2016 |
Authors | Hahn, A, Parey, K, Bublitz, M, Mills, DJ, Zickermann, V, Vonck, J, Kühlbrandt, W, Meier, T |
Journal | Mol Cell |
Volume | 63 |
Issue | 3 |
Pagination | 445-56 |
Date Published | 2016 Aug 04 |
ISSN | 1097-4164 |
Abstract | 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 a strong membrane curvature of ∼100°. Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology. |
DOI | 10.1016/j.molcel.2016.05.037 |
Alternate Journal | Mol. Cell |
Citation Key | 10.1016/j.molcel.2016.05.037 |
PubMed ID | 27373333 |
PubMed Central ID | PMC4980432 |