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Structure of the dimeric ATP synthase from bovine mitochondria

2020; National Academy of Sciences; Volume: 117; Issue: 38 Linguagem: Inglês

10.1073/pnas.2013998117

1091-6490

T.E. Spikes, M.G. Montgomery, John E. Walker,

Photosynthetic Processes and Mechanisms

Significance Adenosine triphosphate (ATP), the fuel of life, is produced in inner membranes of the mitochondria of eukaryotic cells by an embedded molecular machine with a rotary action, called ATP synthase. Single ATP synthases associate into dimers and form long rows, influencing the formation of characteristic cristae which change shape constantly. Our structure of bovine dimers has a wedge made of small proteins and specific lipids in the membrane domain of each monomer that imposes a range of acute angles on the central axes of the monomers, and a pivot between the wedges accommodates rocking motions of the machine accompanying catalysis and other movements that happen independently. It also throws light on how the membrane rotor is made to turn.