Making ATP.
We present a mesoscopic model for ATP synthesis by F(1)F(o) ATPase. The model combines the existing experimental knowledge of the F(1) enzyme into a consistent mathematical model that illuminates how the stages in synthesis are related to the protein structure. For example, the model illuminates how specific interactions between the gamma, epsilon, and alpha(3)beta(3) subunits couple the F(o) motor to events at the catalytic sites. The model also elucidates the origin of ADP inhibition of F(1) in its hydrolysis mode. The methodology we develop for constructing the structure-based model should prove useful in modeling other protein motors.
Xing
Jianhua
J
Departments of Molecular Cell Biology, University of California, Berkeley, CA 94720-1132, USA.
Liao
Jung-Chi
JC
Oster
George
G
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000096:biosynthesis* / Q000378:metabolism; D020134:Catalytic Domain; D006868:Hydrolysis; D008962:Models, Theoretical; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases