Conformational Transition from Catalytic Dwell to ATP-Binding Dwell in F1-ATPase

Abstract

F1-ATPase (F1) is the catalytic part of ATP synthase that synthesizes most of ATP in living organisms. Extensive crystallographic and single-molecule studies have clarified atomic structures and mechanochemical coupling of this unique rotary motor, respectively. However, connection between these two aspects are not well established: structural basis of the functional cycle has been controversial. Here, we use principal component analysis and molecular dynamics simulation to clarify conformational cycle of the molecular motor, integrating information from recent crystallographic and single-molecule studies. Particularly, we resolve conformational transition from the catalytic dwell to the ATP-binding dwell that involves a 40 degree rotation of the rotor.