Speaker
Dr
Daniela Stock
(Victor Chang Cardiac Research Institute)
Description
Rotary ATPases are ubiquitous protein complexes that couple the translocation of protons through membranes to the synthesis or hydrolysis of ATP and are thus central to biological energy conversion. Eukaryotic F-type ATP synthases use energy stored in transmembrane proton gradients to synthesise the biological energy carrier ATP from ADP and inorganic phosphate. The evolutionary related V-type ATPases operate in reverse by utilising energy derived from ATP hydrolysis to build up transmembrane ion gradients thereby enabling transport processes across membranes. Most eubacteria have F-type ATPases, but some eubacteria and all known archaea have ATPases of the A-type, which are close homologues of V-ATPases. A-ATPases are simpler in design than their eukaryotic counterparts, but are bifunctional and can operate in either direction in dependence of their cellular environment (1).
We are using a combination of X-ray structure analysis, electron microscopy and other biochemical and biophysical techniques to obtain a pseudo-atomic model of an A-ATPase (2, 3). In addition, X-ray structures in different conformations along with normal mode analysis suggest a greater dynamics of the intact complex than previously envisioned. This might be important for cooperativity and regulation of intact rotary ATPases (4, 5).
1. Stewart et al. BioArchitecture 3 (2013)
2. Zhou, et al. Science 334, 380-385 (2011)
3. Lee, et al. Nat. Struct. Mol. Biol. 17, 373-378 (2010)
4. Stewart, et al. Nature Communications 3, 687 (2012)
5. Stewart et al. Current Opinion Structural Biology 25, 40-48 (2014)
| Keywords or phrases (comma separated) | X-ray crystallography, electron microscopy, bioenergetics, ATP synthase |
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Primary author
Dr
Daniela Stock
(Victor Chang Cardiac Research Institute)
Co-authors
Dr
Alastair Stewart
(Victor Chang Cardiac Research Institute)
Dr
Lawrence Lee
(Victor Chang Cardiac Research Institute)
