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High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase

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Matthies,  Doreen
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

Klyszejko,  Adriana L.
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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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence Macromolecular Complexes, Max-von-Laue-Str. 15;

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Zitation

Matthies, D., Zhou, W., Klyszejko, A. L., Anselmi, C., Yildiz, Ö., Brandt, K., et al. (2014). High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase. Nature Communications, 5: 5286. doi:10.1038/ncomms6286.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0025-78F4-B
Zusammenfassung
All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is coupled to the transmembrane flow of H(+) or Na(+). Physiologically, however, F/A-type enzymes specialize in ATP synthesis driven by downhill ion diffusion, while eukaryotic V-type ATPases function as ion pumps. To begin to rationalize the molecular basis for this functional differentiation, we solved the crystal structure of the Na(+)-driven membrane rotor of the Acetobacterium woodii ATP synthase, at 2.1 Å resolution. Unlike known structures, this rotor ring is a 9:1 heteromer of F- and V-type c-subunits and therefore features a hybrid configuration of ion-binding sites along its circumference. Molecular and kinetic simulations are used to dissect the mechanisms of Na(+) recognition and rotation of this c-ring, and to explain the functional implications of the V-type c-subunit. These structural and mechanistic insights indicate an evolutionary path between synthases and pumps involving adaptations in the rotor ring.