Research Article

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

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Science  21 Jun 2019:
Vol. 364, Issue 6446, eaaw9128
DOI: 10.1126/science.aaw9128

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Flexible domains in a well-oiled machine

Motors convert one form of energy into another. For biological motors, adenosine triphosphate (ATP) serves as chemical energy and its hydrolysis is coupled to conformational changes that exert mechanical force. ATP synthases reverse this process in a multistep process: first converting an electrochemical gradient to rotational kinetic energy, and then coupling rotation to formation of high-energy phosphodiester bonds. Murphy et al. investigated these energy changes in the dimeric mitochondrial F1-Fo ATP synthase from Polytomella sp., a unicellular alga. They solved high-resolution cryo–electron microscopy structures of the ATP synthase complex, extracting 13 rotational substates. This collection of structures revealed that the rotation of the Fo ring and central stalk is coupled with partial rotations of the F1 head. This flexibility may enable the head to better couple continuous rotation with discrete ATP synthesis events.

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