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Numerical study of the coupling between F-0 with varied numbers of c-subunits and F-1 in an ATP synthase

ATP synthase is a rotary motor which is composed of two portions: the 'rotor' F-0, consisting of a c-ring, and the 'stator' F-1, consisting of an alpha(3)beta(3) hexamer. In different species, the number of c-subunits which form the c-ring is varied from 10 to 14, whereas the alpha(3)beta(3) hexamer is fixed to be 3-fold symmetrical. We have numerically studied the rotational coupling between F-0 with varied number of c-subunits and F-1. It is found that, for any number of c-subunits, the rotor F-0 advances 3 steps per revolution on average, which is determined by the period of F-1, whereas the exact angular pausing positions are determined by the period of F-0. When the symmetry of the c-ring of F-0 is matched with the 3-fold symmetry of F-1, the three steps have equivalent sizes. If not matched, the three steps become nonequivalent: both the step size and average dwell time are different for these steps.