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Engineering rotor ring stoichiometries in the ATP synthase

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

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Klyszejko,  Adriana
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Biotechnology Center, Dresden University of Technology, 01307 Dresden;

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Krasnoselska,  Ganna O.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Heller,  Eva-Maria
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Leone,  Vanessa
Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Vonck,  Janet
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, 60438 Frankfurt am Main, Germany;

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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Pogoryelov, D., Klyszejko, A., Krasnoselska, G. O., Heller, E.-M., Leone, V., Langer, J. D., et al. (2012). Engineering rotor ring stoichiometries in the ATP synthase. Proceedings of the National Academy of Sciences of the United States of America, 109(25), E1599-E1608. doi:10.1073/pnas.1120027109.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-D5BB-4
Zusammenfassung
ATP synthase membrane rotors consist of a ring of c-subunits whose stoichiometry is constant for a given species but variable across different ones. We investigated the importance of c/c-subunit contacts by site-directed mutagenesis of a conserved stretch of glycines (GxGxGxGxG) in a bacterial c11 ring. Structural and biochemical studies show a direct, specific influence on the c-subunit stoichiometry, revealing c< 11, c12, c13, c14, and c> 14 rings. Molecular dynamics simulations rationalize this effect in terms of the energetics and geometry of the c-subunit interfaces. Quantitative data from a spectroscopic interaction study demonstrate that the complex assembly is independent of the c-ring size. Real-time ATP synthesis experiments in proteoliposomes show the mutant enzyme, harboring the larger c12 instead of c11, is functional at lower ion motive force. The high degree of compliance in the architecture of the ATP synthase rotor offers a rationale for the natural diversity of c-ring stoichiometries, which likely reflect adaptations to specific bioenergetic demands. These results provide the basis for bioengineering ATP synthases with customized ion-to-ATP ratios, by sequence modifications.