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A Zhou, A Rohou, DG Schep, JV Bason, MG Montgomery, JE Walker, N Grigorieff and JL Rubinstein
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-inserted F0 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 F0 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 F0 region support a Brownian ratchet mechanism for proton-translocation driven rotation in ATP synthases.
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Concepts
Protein subunit, Cell, Cellular respiration, DNA, Photosynthesis, Mitochondrion, ATP synthase, Adenosine triphosphate
MeSH headings
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