Research Project
Grant-in-Aid for Challenging Exploratory Research
Mitochondrial FoF1-ATP synthase is central to energy conversion in all mammalian cells and employs a highly efficient mechanism of rotary catalysis to recycle cellular ATP from ADP and Pi. The structural basis for the efficient coupling between membrane bound Fo domain and matrix F1 domain remains unresolved due to the absence of X-ray crystal structures of the intact enzyme and the difficulty of visualizing large scale movements by X-ray crystallography in general. Here we took up the challenge of using the emerging technique of single particle cryo-EM to tacke this important biological problem. Purification of the bovine enzyme from cow heart muscle tissue was successfully established yielding more than 100 mg of excellent sample on a reproducible basis. A novel sample preparation approach named GraDeR was developed and successfully applied to monomeric bovine FoF1 ATP synthase and first structures obtained at a resolution of ~11 Angstrom.
All 2016 2015 Other
All Journal Article (5 results) (of which Int'l Joint Research: 3 results, Peer Reviewed: 5 results, Open Access: 4 results, Acknowledgement Compliant: 3 results) Presentation (12 results) (of which Int'l Joint Research: 7 results, Invited: 9 results) Remarks (1 results)
生化学
Volume: 88 Issue: 4 Pages: 532-536
10.14952/SEIKAGAKU.2016.880532
40020948610
Microscopy
Volume: 65 Issue: 3 Pages: 263-267
10.1093/jmicro/dfv381
BBA - Bioenergetics
Volume: in press Issue: 8 Pages: 1191-1196
10.1016/j.bbabio.2016.03.008
Structure
Volume: 23 Issue: 9 Pages: 1769-1775
10.1016/j.str.2015.06.029
eLIFE
Volume: 06119 Pages: 1-36
10.7554/elife.06119
https://grader-protocol.com/
