Fig. 3: Multiplicity of state transitions in the ATPase motor during substrate translocation.
From: Nonequilibrium chemomechanical transduction of ATP-driven protein unfolding in the 26S proteasome
Transition probabilities between 31 conformations H1-H31 obtained from stochastic simulations at ATP concentrations of 0.01 mM (a) and 1 mM (b), respectively. Probabilities of nucleotide state changes obtained by counting the random events of ATP binding, unbinding, and hydrolysis, and ADP unbinding immediately before major conformational transitions occur, at ATP concentrations of 0.01 mM (c) and 1 mM (d), respectively. For each type of nucleotide change listed on the horizontal axis, the six RPTs are arranged according to their distances to the core particle by spreading out the motor subunits anticlockwise, starting with the substrate-engaged RPT at position 1 in the first place. e, f Four predominant pathways of state transitions adopted by the ATPase motor to translocate the substrate peptide, derived from the results in (a–d).
