Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, NSW, Australia.
School of Clinical Medicine, Faculty of Medicine and Health, UNSW Sydney, Sydney, NSW, Australia.
Commun Biol. 2023 Jan 11;6(1):26. doi: 10.1038/s42003-023-04414-z.
FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli FF ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε.
FF ATP 合酶作为一种生物发电机，对细胞能量产生有重要贡献。质子流引起 F 马达的旋转，这种旋转传递到 F 马达以催化 ATP 的产生，而灵活的 F/F 偶联对于高效催化是必需的。FF ATP 合酶也可以反向运作，水解 ATP 并泵送质子，在细菌中，这种功能可以通过抑制性 ε 亚基进行调节。在这里，我们展示了 cryo-EM 数据，显示了在与 10mM MgATP 孵育后，处于不同旋转和抑制亚状态的大肠杆菌 FF ATP 合酶。我们的结构表明，抑制性 ε 亚基内的结构转变如何诱导中心茎的扭转运动，从而使其能够在 F 马达内旋转。这突出了中央转子对于 F 和 F 马达的灵活偶联的重要性，并进一步深入了解由亚基 ε 介导的调节机制。
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