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-Structure paper
Title | Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. |
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Journal, issue, pages | Mol Cell, Vol. 63, Issue 3, Page 445-456, Year 2016 |
Publish date | Aug 4, 2016 |
Authors | Alexander Hahn / Kristian Parey / Maike Bublitz / Deryck J Mills / Volker Zickermann / Janet Vonck / Werner Kühlbrandt / Thomas Meier / |
PubMed 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 ...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. |
External links | Mol Cell / PubMed:27373333 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.5 - 9.6 Å |
Structure data | EMDB-8151: EMDB-8152: EMDB-8153: EMDB-8154: EMDB-8155: PDB-5fl7: |
Chemicals | ChemComp-ATP: ChemComp-MG: ChemComp-ADP: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / ATP SYNTHASE FAMILY / NUCLEOTIDE BINDING / PROTON TRANSPORTING / ROTATIONAL MECHANISM / ATP BIOSYNTHETIC PROCESS / ATP SYNTHESIS/HYDROLYSIS |