Rotating with the brakes on and other unresolved features of the vacuolar ATPase. (9th June 2016)

• Record Type: Journal Article
• Authors: Rawson, Shaun; Harrison, Michael A.; Muench, Stephen P.
• Is Part Of: Biochemical Society transactions. Volume 44:Number 3(2016)
• Page Start: 851
• Page End: 855
• Publication Date: 2016-06-09
• Subjects: cryo-EM -- molecular motor -- rotary ATPase -- vacuolar ATPase; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20160043
• Languages: English
• ISSNs: 0300-5127

Abstract

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.