Structure of V-ATPase from the mammalian brain
Autor: | Teresa Rodrigues, John Rubinstein, Antje Voelker, Silvia Frisia, Jon Woodhead, Carol Robinson |
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Rok vydání: | 2020 |
Předmět: |
Vacuolar Proton-Translocating ATPases
Protein subunit Receptors Cell Surface Synaptic vesicle Article Renin-Angiotensin System Cell membrane 03 medical and health sciences Bacterial Proteins Protein Domains Membrane region medicine Animals V-ATPase Wnt Signaling Pathway 030304 developmental biology ATP6AP2 0303 health sciences Multidisciplinary Chemistry Cell Membrane Cryoelectron Microscopy 030302 biochemistry & molecular biology Brain Transmembrane protein Rats Cell biology medicine.anatomical_structure Models Chemical Membrane protein Biocatalysis Biomarkers |
Zdroj: | Science |
ISSN: | 1095-9203 0036-8075 |
Popis: | 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 |
Databáze: | OpenAIRE |
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