Fig. 7: Proton translocation pathway in P. aeruginosa ATP Synthase. | Nature Communications

Fig. 7: Proton translocation pathway in P. aeruginosa ATP Synthase.

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

Fig. 7

a The cryo-EM map reveals moderate resolution features within the Fo-motor, highlighting a periplasmic channel (P) and a cytoplasmic channel (C) that connect to the interior of the molecule. Residue Arg221 of subunit a (blue) is positioned between these two channels. The cytoplasmic channel is capped. Map shown at 8σ. b Surface representation of the molecular model illustrates two pores at the periplasmic protonation and cytoplasmic deprotonation sites. c In synthesis mode, protons from the periplasmic channel bind to residue cAsp60 of a c subunit (grey/CPK spheres) and rotate approximately 288° (8/10 c-ring rotation) before reaching the cytoplasmic channel. Residue aArg221 of subunit a prevents short-circuiting, ensuring the motor rotates anticlockwise (when viewed from the F1-ATPase). Map shown at 8σ and rotated relative to (a, b), as viewed from the F1-ATPase.

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