<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rawson S</submitter><funding>Medical Research Council</funding><pagination>851-5</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4900747</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>44(3)</volume><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.</pubmed_abstract><journal>Biochemical Society transactions</journal><pubmed_title>Rotating with the brakes on and other unresolved features of the vacuolar ATPase.</pubmed_title><pmcid>PMC4900747</pmcid><funding_grant_id>G1000567</funding_grant_id><pubmed_authors>Rawson S</pubmed_authors><pubmed_authors>Muench SP</pubmed_authors><pubmed_authors>Harrison MA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Rotating with the brakes on and other unresolved features of the vacuolar ATPase.</name><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.</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jun</publication><modification>2025-04-29T10:04:28.367Z</modification><creation>2020-10-29T09:21:53Z</creation></dates><accession>S-EPMC4900747</accession><cross_references><pubmed>27284051</pubmed><doi>10.1042/BST20160043</doi></cross_references></HashMap>