Dataset Information
Cryo-EM structures of human V-ATPase
Ontology highlight
ABSTRACT:
SUBMITTER: Longfei Wang
PROVIDER: EMPIAR-11132 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
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]