|Title||Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.|
|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 Å|
|Keywords||ATP synthase / rotary ATPase / Animals / Cattle / Computational Biology / Cryoelectron Microscopy / Imaging, Three-Dimensional / Mitochondrial Proton-Translocating ATPases / Models, Molecular / Protein Conformation / Protein Folding / HYDROLASE|
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