{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rawson S"],"funding":["Medical Research Council"],"pagination":["851-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4900747"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["44(3)"],"pubmed_abstract":["The rotary ATPase family comprises the ATP synthase (F-ATPase), vacuolar ATPase (V-ATPase) and archaeal ATPase (A-ATPase). These either predominantly utilize a proton gradient for ATP synthesis or use ATP to produce a proton gradient, driving secondary transport and acidifying organelles. With advances in EM has come a significant increase in our understanding of the rotary ATPase family. Following the sub nm resolution reconstructions of both the F- and V-ATPases, the secondary structure organization of the elusive subunit a has now been resolved, revealing a novel helical arrangement. Despite these significant developments in our understanding of the rotary ATPases, there are still a number of unresolved questions about the mechanism, regulation and overall architecture, which this mini-review aims to highlight and discuss."],"journal":["Biochemical Society transactions"],"pubmed_title":["Rotating with the brakes on and other unresolved features of the vacuolar ATPase."],"pmcid":["PMC4900747"],"funding_grant_id":["G1000567"],"pubmed_authors":["Rawson S","Muench SP","Harrison MA"],"additional_accession":[]},"is_claimable":false,"name":"Rotating with the brakes on and other unresolved features of the vacuolar ATPase.","description":"The rotary ATPase family comprises the ATP synthase (F-ATPase), vacuolar ATPase (V-ATPase) and archaeal ATPase (A-ATPase). These either predominantly utilize a proton gradient for ATP synthesis or use ATP to produce a proton gradient, driving secondary transport and acidifying organelles. With advances in EM has come a significant increase in our understanding of the rotary ATPase family. Following the sub nm resolution reconstructions of both the F- and V-ATPases, the secondary structure organization of the elusive subunit a has now been resolved, revealing a novel helical arrangement. Despite these significant developments in our understanding of the rotary ATPases, there are still a number of unresolved questions about the mechanism, regulation and overall architecture, which this mini-review aims to highlight and discuss.","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2025-04-29T10:04:28.367Z","creation":"2020-10-29T09:21:53Z"},"accession":"S-EPMC4900747","cross_references":{"pubmed":["27284051"],"doi":["10.1042/BST20160043"]}}