Figure 6 : Comparison of M-PPases with ATPases, demonstrating the formal similarity and the coupling of Lys/Arg motion to ion pumping.

From: Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism

Figure 6

(a) Proton pumping and peristaltic motion of K16.50 in VrPPase and (b) sodium pumping and peristaltic motion of K16.50 in TmPPase. (c) Structural overview and hypothesized proton transport mechanism of P-type ATPases31. (d) Proton pumping and rotary motion in F-ATPase29: (based on figure 6 from reference 29) in the hydrolysis direction. Colour scheme: green, initial residue states; yellow, intermediate states; magenta, final states; blue before and after (F-ATPase). D6.50 and E6.53 in (b) and the helices in (a,b) are coloured as in Figs 2 and 3 to emphasize the fact that the motions there are relatively small. Numbers represent order of ion progression through the respective ion channels.