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Showing 1–7 of 7 results
Advanced filters: Author: Meghna Sobti Clear advanced filters

  • F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the Fo motor cring that reveals the mechanism of elastic coupling between the two rotary motors, which is essential for effective ATP synthesis.

    • Meghna Sobti
    • James L. Walshe
    • Alastair G. Stewart
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • F1Fo ATP synthase works using a rotary catalysis mechanism. Here, the authors report cryo-EM structures of Bacillus PS3 F1-ATPase encompassing the complete set of six states taken up during the catalytic cycle, including the binding- and catalytic-dwell states.

    • Meghna Sobti
    • Hiroshi Ueno
    • Alastair G. Stewart
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10