Abstract
Significance In cells, chemical energy is interconverted with electrochemical ion gradients across membranes for numerous processes. Three of the most significant enzymes that carry out this conversion are known as rotary ATPases because ion translocation is coupled to the synthesis or hydrolysis of ATP by rotation of part of the enzyme. These protein assemblies are the closely related eukaryotic V-ATPases and bacterial or archaeal V/A-ATPases, and the more distantly related F-type ATP synthases. Understanding of rotary ATPases has been limited by not knowing the structure of the subunit that couples ion translocation to rotation. Here, we determine the structure of this subunit for two of the three types of rotary ATPases, identifying a conserved architecture and mechanism in all three enzymes.
Keywords
Thermus thermophilusATPaseProtein subunitV-ATPaseBiologyF-ATPaseATP synthase gamma subunitSaccharomyces cerevisiaeBiochemistryATP hydrolysisATP synthaseAAA proteinsEnzymeYeastGeneEscherichia coli
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Publication Info
- Year
- 2016
- Type
- article
- Volume
- 113
- Issue
- 12
- Pages
- 3245-3250
- Citations
- 50
- Access
- Closed
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Daniel Schep,
Jianhua Zhao,
John L. Rubinstein
(2016).
Models for the a subunits of the <i>Thermus thermophilus</i> V/A-ATPase and <i>Saccharomyces cerevisiae</i> V-ATPase enzymes by cryo-EM and evolutionary covariance.
Proceedings of the National Academy of Sciences
, 113
(12)
, 3245-3250.
https://doi.org/10.1073/pnas.1521990113
Identifiers
- DOI
- 10.1073/pnas.1521990113