Rawson, S, Harrison, MA and Muench, SP orcid.org/0000-0001-6869-4414 (2016) Rotating with the brakes on and other unresolved features of the vacuolar ATPase. Biochemical Society Transactions, 44 (3). pp. 851-855. ISSN 0300-5127
Abstract
The rotary ATPase family is comprised of the ATP synthase (F-ATPase), vacuolar ATPase (V-ATPase) and acrahael ATPase (A-ATPase). These either predominantly utilise a proton gradient for ATP synthesis or use ATP to produce a proton gradient, driving secondary transport and acidifying organelles. With advances in electron microscopy (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-ATPase the secondary structure organisation 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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2016 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY). |
Keywords: | cryo-EM, molecular motor, rotary ATPase, vacuolar ATPase |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Funding Information: | Funder Grant number MRC G1000567/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 19 May 2016 10:20 |
Last Modified: | 23 Jun 2023 22:06 |
Published Version: | http://dx.doi.org/10.1042/BST20160043 |
Status: | Published |
Publisher: | Portland Press |
Identification Number: | 10.1042/BST20160043 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:99866 |