Unknown

Dataset Information

0

Rotating with the brakes on and other unresolved features of the vacuolar ATPase.


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.

SUBMITTER: Rawson S 

PROVIDER: S-EPMC4900747 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Rotating with the brakes on and other unresolved features of the vacuolar ATPase.

Rawson Shaun S   Harrison Michael A MA   Muench Stephen P SP  

Biochemical Society transactions 20160601 3


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 organi  ...[more]

Similar Datasets

| S-EPMC4646912 | biostudies-literature
| S-EPMC12705107 | biostudies-literature
| S-EPMC4447986 | biostudies-literature
| S-EPMC2602884 | biostudies-literature
| S-EPMC4646367 | biostudies-literature
| S-EPMC12691628 | biostudies-literature
| S-EPMC2812417 | biostudies-literature