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Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling

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Murphy,  Bonnie J.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Klusch,  Niklas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mills,  Deryck
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Murphy, B. J., Klusch, N., Langer, J. D., Mills, D., Yildiz, Ö., & Kühlbrandt, W. (2019). Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling. Science, 364(6446): eaaw9128, pp. 1155. doi:10.1126/science.aaw9128.


Cite as: http://hdl.handle.net/21.11116/0000-0003-E0E5-D
Abstract
F1-Fo-adenosine triphosphate (ATP) synthases make the energy of the proton-motive force available for energy-consuming processes in the cell. We determined the single-particle cryo-electron microscopy structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at a resolution of 2.7 to 2.8 angstroms. Separation of 13 well-defined rotary substates by three-dimensional classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30° of each 120° primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F1 and Fo subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit. A conserved metal ion in the proton access channel may synchronize c-ring protonation with rotation.