The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Open accessAbstract
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.
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Cites
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Protein 3D Structure Computed from Evolutionary Sequence Variation
Marks, D. S., Colwell, L. J., Sheridan, R., Hopf, T. A., Pagnani, A., Zecchina, R., & Sander, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028766 · Cited by 1,144
The ATP synthase: the understood, the uncertain and the unknown
Walker, J. E. (2013) · Biochemical Society Transactions · doi:10.1042/bst20110773 · Cited by 614
Self-citationOligomycin Frames a Common Drug-Binding Site in the ATP Synthase
Symersky, J., Osowski, D., Walters, D. E., & Mueller, D. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207912109 · Cited by 269
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Assembly of mammalian oxidative phosphorylation complexes I–V and supercomplexes
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He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251
Self-citationAtomic model for the dimeric F O region of mitochondrial ATP synthase
Guo, H., Bueler, S. A., & Rubinstein, J. L. (2017) · Science · doi:10.1126/science.aao4815 · Cited by 225
Self-citationStructure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline
Guo, H., Courbon, G. M., Bueler, S. A., Mai, J., Liu, J., & Rubinstein, J. L. (2021) · Nature · doi:10.1038/s41586-020-3004-3 · Cited by 200
Self-citationHe, J., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711201114 · Cited by 182
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Metadata
- Authors
- Zhou, A., Rohou, A., Schep, D. G., Bason, J. V., Montgomery, M. G., Walker, J. E., Grigorieff, N., & Rubinstein, J. L.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2015-10-06
- Volume
- 4
- Pages
- e10180-e10180
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W2275524693
- Cited by
- 296
- References
- 4
- FWCI
- 15.82
- Type
- journal article
- Language
- en
- Open access
- gold
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