5ARA
Bovine mitochondrial ATP synthase state 1a
Summary for 5ARA
| Entry DOI | 10.2210/pdb5ara/pdb |
| Related | 5ARE 5ARH 5ARI 5FIJ 5FIK 5FIL |
| EMDB information | 3164 |
| Descriptor | ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (11 entities in total) |
| Functional Keywords | hydrolase, atp synthase, rotary atpase |
| Biological source | BOS TAURUS (COW) More |
| Cellular location | Mitochondrion inner membrane : P19483 Mitochondrion: P02721 P00829 P05631 P05630 P05632 P13621 P13619 P13620 Mitochondrion inner membrane; Multi-pass membrane protein: P00847 Mitochondrion membrane; Multi-pass membrane protein: P32876 |
| Total number of polymer chains | 22 |
| Total formula weight | 518892.57 |
| Authors | Zhou, A.,Rohou, A.,Schep, D.G.,Bason, J.V.,Montgomery, M.G.,Walker, J.E.,Grigorieff, N.,Rubinstein, J.L. (deposition date: 2015-09-24, release date: 2015-10-14, Last modification date: 2024-05-08) |
| Primary citation | Zhou, A.,Rohou, A.,Schep, D.G.,Bason, J.V.,Montgomery, M.G.,Walker, J.E.,Grigorieff, N.,Rubinstein, J.L. Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. Elife, 4:e10180-e10180, 2015 Cited by PubMed Abstract: 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. PubMed: 26439008DOI: 10.7554/eLife.10180 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.4 Å) |
Structure validation
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