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Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM

TitleStructure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Publication TypeJournal Article
Year of Publication2015
AuthorsZhou, A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL
Refereed DesignationRefereed
JournaleLife
Volume4
Issuee10180
Pagination1-15
Date Published10/2015
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 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.

DOI10.7554/eLife.10180
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