@article {Zhou023770, author = {Anna Zhou and Alexis Rohou and Daniel G. Schep and John V. Bason and Martin G. Montgomery and John E. Walker and Nikolaus Grigorieff and John L. Rubinstein}, title = {Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM}, elocation-id = {023770}, year = {2015}, doi = {10.1101/023770}, publisher = {Cold Spring Harbor Laboratory}, 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-bound FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor. Here we report 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 different states of the enzyme that show different modes of bending and twisting of 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.}, URL = {https://www.biorxiv.org/content/early/2015/08/11/023770}, eprint = {https://www.biorxiv.org/content/early/2015/08/11/023770.full.pdf}, journal = {bioRxiv} }