Abstract
Rotary ATPases are unique rotary molecular motors that function as energy conversion machines. Among all known rotary ATPases, F(1)-ATPase is the best characterized rotary molecular motor. There are many high-resolution crystal structures and the rotation dynamics have been investigated in detail by extensive single-molecule studies. In contrast, knowledge on the structure and rotation dynamics of V(1)-ATPase, another rotary ATPase, has been limited. However, recent high-resolution structural studies and single-molecule studies on V(1)-ATPase have provided new insights on how the catalytic sites in this molecular motor change its conformation during rotation driven by ATP hydrolysis. In this review, we summarize recent information on the structural features and rotary dynamics of V(1)-ATPase revealed from structural and single-molecule approaches and discuss the possible chemomechanical coupling scheme of V(1)-ATPase with a focus on differences between rotary molecular motors.