Fig. 5: Dimer interfaces are scattered throughout the Fo-subcomplex. | Nature Communications

Fig. 5: Dimer interfaces are scattered throughout the Fo-subcomplex.

From: Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

Fig. 5

a Overview of ATP synthase dimer structure with Fo subunits participating in dimer interfaces shown with their respective colors. Windows indicate regions shown in panels b-d close-up views. b The extended C-terminal domain of subunit-k engages in several dimer interface interactions below the c-ring with Fo subunits ATPTT5-8′. A bound cardiolipin (CDL, red) mediates interactions between subunit-k and ATPTT6′. c Subunits b and b′ form a hydrophobic dimer interface with cardiolipins (CDL, red). Cardiolipin density is carved 2.6 Å around atoms in Fo-dimer local-resolution filtered map. d Subunits f and f′ form a dimer interface through electrostatic, polar and hydrophobic interactions.

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