Structure of dimeric ATP synthase from the inner membrane of yeast mitochondria

Research report (imported) 2016 - Max Planck Institute of Biophysics

Authors
Hahn, Alexander; Parey, Kristian; Bublitz, Maike; Mills, Deryck J.; Zickermann, Volker; Vonck, Janet; Kühlbrandt, Werner; Meier, Thomas
Departments
Strukturbiologie
DOI
Summary
We determined the structure of a complete, dimeric F1Fo-ATP synthase from mitochondria of the yeast Yarrowia lipolytica by a combination of cryo-electron microscopy (cryo-EM) and X-ray crystallography. The structure resolves 58 of the 60 subunits in the dimer. 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. Our data explain the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.

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