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

Doreen Matthies, Wenchang Zhou, Adriana L. Klyszejko, Claudio Anselmi, Özkan Yildiz, Karsten Brandt, Volker Müller, José D. Faraldo-Gómez () and Thomas Meier ()
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Doreen Matthies: Max Planck Institute of Biophysics
Wenchang Zhou: Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health
Adriana L. Klyszejko: Max Planck Institute of Biophysics
Claudio Anselmi: Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health
Özkan Yildiz: Max Planck Institute of Biophysics
Karsten Brandt: Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt am Main
Volker Müller: Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt am Main
José D. Faraldo-Gómez: Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health
Thomas Meier: Max Planck Institute of Biophysics

Nature Communications, 2014, vol. 5, issue 1, 1-14

Abstract: Abstract 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.

Date: 2014
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DOI: 10.1038/ncomms6286

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