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ATP synthase (F1F0-ATPase) is ubiquitous in nature and is the source of the proton gradient that is used for driving ATP synthesis. How these protein complexes are assembled into a membranous nanomotor is still unclear. Recent studies have shown that the F1F0-ATPase of Chlamydomonas reinhardtii CCMP2230 is made as a complex of eight subunits that are linked by a series of tight membrane-bound contacts at the peripheral stalk region. Here, we present three-dimensional reconstructed models of the ATP synthase complex, where each subunit is rendered in a continuous helical structure. The eight subunits assemble into two helical ‘propellers’ of opposite handedness. In the membrane proximal regions of the shafts, the eight subunits form an asymmetric array which results in an antiparallel ‘double-helical’ structure. The essential interaction sites between the subunits are also revealed and are broadly consistent with the results of earlier studies on isolated ATP synthase. Furthermore, the ‘double-helical’ structure is accommodated by a defined arrangement of transmembrane domains, suggesting that it may be functionally adapted to support a proton channel and to clamp at the membrane in the intact enzyme.Vitex philippinensis

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