{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Abbas YM"],"funding":["European Research Council","The Hospital For Sick Children","Wellcome Trust","Canadian Institutes of Health Research","CIHR","Canada Research Chairs"],"pagination":["1240-1246"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7324285"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["367(6483)"],"pubmed_abstract":["In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a <i>Legionella pneumophila</i> effector protein. Cryo-electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in bot"],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Structure of V-ATPase from the mammalian brain."],"pmcid":["PMC7324285"],"funding_grant_id":["695511","PJT166152","104633/Z/14/Z","104633","Postdoctoral Fellowship","69551-ENABLE"],"pubmed_authors":["Abbas YM","Rubinstein JL","Bueler SA","Wu D","Robinson CV"],"additional_accession":[]},"is_claimable":false,"name":"Structure of V-ATPase from the mammalian brain.","description":"In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a <i>Legionella pneumophila</i> effector protein. Cryo-electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in bot","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2026-05-03T04:48:47.272Z","creation":"2020-09-15T07:23:23Z"},"accession":"S-EPMC7324285","cross_references":{"pubmed":["32165585"],"doi":["10.1126/science.aaz2924"]}}