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Cryo-EM structures of human V-ATPase

ABSTRACT:

SUBMITTER: Longfei Wang

PROVIDER: EMPIAR-11132 | biostudies-other |

REPOSITORIES: biostudies-other

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Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.

Wang Longfei L Wu Di D Robinson Carol V CV Wu Hao H Fu Tian-Min TM

Molecular cell 20201015 3

Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V<sub>1</sub> complex for ATP hydrolysis and a membrane-embedded V<sub>o</sub> complex for proton transfer. They play important roles in acidification of intracellular vesicles, organelles, and the extracellular milieu in eukaryotes. Here, we report cryoelectron microscopy structures of human V-ATPase in three rotational states at up to 2.9-Å resolution. Aided by mass spectrom ...[more]

PMID: 33065002

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