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Structure of V-ATPase from the mammalian brain

Y.M. Abbas, Di Wu, Stephanie A. Bueler, Carol V. Robinson, John L. Rubinstein

2020Science253 citationsDOIOpen Access PDF

Abstract

Snapshots of a rotary pump Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-hydrolysis–driven proton pumps. In neurons, V-ATPase activity generates a proton gradient across the membrane of synaptic vesicles so that neurotransmitters can be loaded into the vesicles. Abbas et al. developed a method to purify V-ATPase from rat brain and determined the structure of the entire complex by cryo–electron microscopy. Native mass spectrometry showed that the preparation was homogeneous and complemented structural studies by confirming the subunit composition. Three rotational states were resolved at better than 4-angstrom resolution, providing insight into the conformational changes that couple ATP hydrolysis to proton pumping. Science , this issue p. 1240

Topics & Concepts

Protein subunitTransmembrane proteinV-ATPaseSynaptic vesicleCell biologyBiologyATPaseGene isoformMembrane proteinTransmembrane domainChemistryBiochemistryMembraneVesicleEnzymeReceptorGeneATP Synthase and ATPases ResearchMitochondrial Function and PathologyMetalloenzymes and iron-sulfur proteins
Structure of V-ATPase from the mammalian brain | Litcius