RT Journal Article
SR Electronic
T1 Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 023770
DO 10.1101/023770
A1 Anna Zhou
A1 Alexis Rohou
A1 Daniel G. Schep
A1 John V. Bason
A1 Martin G. Montgomery
A1 John E. Walker
A1 Nikolaus Grigorieff
A1 John L. Rubinstein
YR 2015
UL http://biorxiv.org/content/early/2015/08/11/023770.abstract
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.