Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus

Cryo EM structure of intact rotary H⁺-ATPase/synthase from Thermus thermophilus

Cryo EM structure of intact rotary H⁺-ATPase/synthase from <i>Thermus thermophilus</i>, Published online: 08 January 2018; doi:10.1038/s41467-017-02553-6

H+-ATPases employ a rotary catalytic mechanism to couple ATP synthesis/hydrolysis with proton translocation through the membrane. Here, the authors use high-resolution cryoEM to characterize three rotational states of a bacterial H+-ATPase, providing a more detailed model of its catalytic mechanism.

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