PT  - JOURNAL ARTICLE
AU  - Anna Zhou
AU  - Alexis Rohou
AU  - Daniel G. Schep
AU  - John V. Bason
AU  - Martin G. Montgomery
AU  - John E. Walker
AU  - Nikolaus Grigorieff
AU  - John L. Rubinstein
TI  - Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
AID  - 10.1101/023770
DP  - 2015 Jan 01
TA  - bioRxiv
PG  - 023770
4099  - http://biorxiv.org/content/early/2015/08/11/023770.short
4100  - http://biorxiv.org/content/early/2015/08/11/023770.full
AB  - 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.