Rotary mechanism of the prokaryotic Vo motor driven by proton motive force

Jun-ichi Kishikawa, Yui Nishida, Atsuki Nakano, Takayuki Kato, Kaoru Mitsuoka, Kei-ichi Okazaki () and Ken Yokoyama ()
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Jun-ichi Kishikawa: Kita-ku
Yui Nishida: Kita-ku
Atsuki Nakano: Kita-ku
Takayuki Kato: Suita
Kaoru Mitsuoka: Osaka University
Kei-ichi Okazaki: National Institutes of Natural Sciences
Ken Yokoyama: Kita-ku

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. However, the mechanism of how pmf converts into c-ring rotation remains unclear. This study presents a 2.8 Å cryo-EM structure of the Vo domain of V/A-ATPase from Thermus thermophilus, revealing precise orientations of glutamate (Glu) residues in the c12-ring. Three Glu residues face a water channel, with one forming a salt bridge with the Arginine in the stator (a/Arg). Molecular dynamics (MD) simulations show that protonation of specific Glu residues triggers unidirectional Brownian motion of the c12-ring towards ATP synthesis. When the key Glu remains unprotonated, the salt bridge persists, blocking rotation. These findings suggest that asymmetry in the protonation of c/Glu residues biases c12-ring movement, facilitating rotation and ATP synthesis.

Date: 2024
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DOI: 10.1038/s41467-024-53504-x

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