5FL7
Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase
Summary for 5FL7
| Entry DOI | 10.2210/pdb5fl7/pdb |
| Descriptor | ATP SYNTHASE SUBUNIT ALPHA, ATP SYNTHASE SUBUNIT BETA, ATP SYNTHASE SUBUNIT GAMMA CHAIN, MITOCHONDRIAL, ... (10 entities in total) |
| Functional Keywords | hydrolase, atp synthase family, nucleotide binding, proton transporting, rotational mechanism, atp biosynthetic process, atp synthesis/hydrolysis |
| Biological source | YARROWIA LIPOLYTICA More |
| Cellular location | Mitochondrion membrane ; Multi- pass membrane protein : Q37695 |
| Total number of polymer chains | 19 |
| Total formula weight | 466474.66 |
| Authors | Parey, K.,Bublitz, M.,Meier, T. (deposition date: 2015-10-22, release date: 2016-06-29, Last modification date: 2024-01-10) |
| Primary citation | Hahn, A.,Parey, K.,Bublitz, M.,Mills, D.J.,Zickermann, V.,Vonck, J.,Kuhlbrandt, W.,Meier, T. Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. Mol.Cell, 63:445-, 2016 Cited by 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 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. PubMed: 27373333DOI: 10.1016/J.MOLCEL.2016.05.037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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