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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RELION: Implementation of a Bayesian approach to cryo-EM structure determination
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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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