[20p-225B-1~5] Frontier of Cryo-Electron Microscopy

[20p-225B-2] Structure and dynamics of ATP synthase revealed by cryogenic electron microscopy

Asuko Nakanishi¹, Jun-ichi Kishikawa¹, Kaoru Mistuoka², 〇Ken Yokoyama¹ (1.Kyoto Sangyo Univ., 2.Osaka Univ.)

Keywords:cryo electron microscopy, ATP synthase, Bioenergetics

ATP synthase couples ATP synthesis from ADP and phosphate with proton flow through the membrane domain with a rotation of the central rotor complex against the surrounding peripheral stator apparatus. In this study, we revealed the whole structure of the V type H⁺-rotary ATP synthase from the bacterium, Thermus thermophilususing cryoEM single particle analysis. Three obtained rotational structures of ATP synthase differ in the orientation of the rotor subunit and provide important insights into how the surrounding stator subunits dynamically deform and reposition during rotation.
Furthermore, we analyzed the both whole complex and V₁domains using image subtraction masking methods, providing the first detailed insight into the contact surface between rotor subunits and peripheral stators, and into molecular basis of structural flexibility of the peripheral stators. In addition, the structure of membrane embedded domain suggests a clear proton translocation path through the V_odomain.