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-Structure paper
タイトル | Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. |
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ジャーナル・号・ページ | Elife, Vol. 4, Page e10180, Year 2015 |
掲載日 | 2015年10月6日 |
![]() | Anna Zhou / Alexis Rohou / Daniel G Schep / John V Bason / Martin G Montgomery / John E Walker / Nikolaus Grigorieff / John L Rubinstein / ![]() ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 6.4 - 9.0 Å |
構造データ | ![]() EMDB-3181: |
由来 |
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![]() | HYDROLASE / ATP SYNTHASE / ROTARY ATPASE |