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-Structure paper
Title | Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. |
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Journal, issue, pages | Elife, Vol. 4, Page e10180, Year 2015 |
Publish date | Oct 6, 2015 |
Authors | Anna Zhou / Alexis Rohou / Daniel G Schep / John V Bason / Martin G Montgomery / John E Walker / Nikolaus Grigorieff / John L Rubinstein / |
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 ...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. |
External links | Elife / PubMed:26439008 / PubMed Central |
Methods | EM (single particle) |
Resolution | 6.4 - 9.0 Å |
Structure data | EMDB-3164, PDB-5ara: EMDB-3165, PDB-5are: EMDB-3166, PDB-5arh: EMDB-3167, PDB-5ari: EMDB-3168, PDB-5fij: EMDB-3169, PDB-5fik: EMDB-3170, PDB-5fil: EMDB-3181: |
Source |
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Keywords | HYDROLASE / ATP SYNTHASE / ROTARY ATPASE |