Fig. 9: Fo-motor conducting sub-states in P. aeruginosa ATP synthase. | Nature Communications

Fig. 9: Fo-motor conducting sub-states in P. aeruginosa ATP synthase.

From: Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy

Fig. 9

Cryo-EM classification of F₁ rotary State 2 resolves two Fo substeps (Fo substep 1 and Fo substep 2) that differ by a ~ 11° rotation of the c-ring (grey) relative to the stator subunit a (orange), as viewed from F1. Left (Fo substep 1): one cAsp60 (sticks) faces the cytoplasmic half-channel (C), enabling proton release (deprotonation). Right (Fo substep 2): the c-ring has rotated ~11° in the synthesis direction (black arrow), bringing a different cAsp60 into alignment with the periplasmic half-channel (P) for proton uptake (protonation). aArg221 is situated between the channels, preventing short circuiting of the motor.

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