Article

Structure of V-ATPase from the mammalian brain

Y.M. AbbasMolecular Medicine Program, The Hospital for Sick Children Research Institute, Toronto, ON M5G 0A4, CanadaDi WuPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UKStephanie A. BuelerMolecular Medicine Program, The Hospital for Sick Children Research Institute, Toronto, ON M5G 0A4, CanadaCarol V. RobinsonPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UKJohn L. RubinsteinDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada

2020en

ABI

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

Identifiers

DOI: 10.1126/science.aaz2924

Citations and references

Cited by 20 references

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