Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
Schep, Daniel G
Bason, John V
Rubinstein, John L
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Zhou, A., Rohou, A., Schep, D. G., Bason, J. V., Montgomery, M., Walker, J., Grigorieff, N., & et al. (2015). Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.. Elife, 4 (e10180)https://doi.org/10.7554/eLife.10180
Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases.
ATP synthase, biochemistry, biophysics, bovine, coevolution, cryo-EM, evolutionary covariance, structural biology, structure, Animals, Cattle, Computational Biology, Cryoelectron Microscopy, Imaging, Three-Dimensional, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Protein Conformation, Protein Folding
External DOI: https://doi.org/10.7554/eLife.10180
This record's URL: https://www.repository.cam.ac.uk/handle/1810/266076
Attribution 4.0 International
Licence URL: http://creativecommons.org/licenses/by/4.0/