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High-resolution structure of the rotor ring of a proton-dependent ATP synthase

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Pogoryelov,  Denys
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Faraldo-Gómez,  José D.
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence Macromolecular Complexes, Max-Planck Institute of Biophysics, Frankfurt am Main, Germany;

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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence Macromolecular Complexes, Max-Planck Institute of Biophysics, Frankfurt am Main, Germany;

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Citation

Pogoryelov, D., Yildiz, Ö., Faraldo-Gómez, J. D., & Meier, T. (2009). High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nature Structural and Molecular Biology, 16(10), 1068-1073. doi:10.1038/nsmb.1678.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D7A7-F
Abstract
The crystal structure of the c-ring from the proton-coupled F1Fo ATP synthase from Spirulina platensis is shown at 2.1-Å resolution. The ring includes 15 membrane-embedded c subunits forming an hourglass-shaped assembly. The structure demonstrates that proton translocation across the membrane entails protonation of a conserved glutamate located near the membrane center in the c subunit outer helix. The proton is locked in this site by a precise hydrogen bond network reminiscent of that in Na+-dependent ATP synthases. However, the structure suggests that the different coordination chemistry of the bound proton and the smaller curvature of the outer helix drastically enhance the selectivity of the H+ site against other cations, including H3O+. We propose a model for proton translocation whereby the c subunits remain in this proton-locked state when facing the membrane lipid. Proton exchange would occur in a more hydrophilic and electrostatically distinct environment upon contact with the a subunit interface.