Fig. 4: ATP binding to the designed site accelerates the rotation rate allosterically.
a, A typical rotation time course of the designed V1 (red) and the wild-type V1 (black)21, at 100 µM ATP. All data for the wild-type V1-ATPase were obtained from ref. 21. The insets show the rotation x,y trajectory. The angle distributions are shown at the bottom. b, [ATP] dependence of rotation rates for the wild-type (black)21, the designed V1 (red), the design mutant K157Q (orange) and the design double-mutant K157A/S158A (magenta). The [ATP] at the most accelerated rotation is highlighted in grey. The rates were plotted with averaged values using three molecules or more (Supplementary Table 1) and the error bars represent the s.d. The black lines are the fitted curves to the Michaelis–Menten equation for the wild-type rotation rates.
