Atomic model for the membrane-embedded motor of a eukaryotic V-ATPase

Atomic model for the membrane-embedded motor of a eukaryotic V-ATPase

In work led by postdoctoral fellow Mohammad T. Mazhab-Jafari, the Rubinstein laboratory used electron cryomicroscopy (cryo-EM) to determine the atomic structure of the membrane-bound region of a eukaryotic V-ATPase. This study, which was published in Nature, gives the first high-resolution structure for the membrane region of any rotary ATPase, a family of enzymes that includes proton pumping V-ATPases and proton-driven ATP synthases. The structure reveals several surprising features of the enzyme, locates the the cytoplasmic half-channel for protons, suggests a mechanism for proton translocation, and identifies a novel subunit of the V-ATPase.