Unwinding the world’s smallest biological rotary motor by degrees

Unwinding the world’s smallest biological rotary motor by degrees

Unwinding the world’s smallest biological rotary motor by degrees
Researchers from Tokyo University of Science reveal that multiple subunits of the ATPase complex act in harmony to achieve the stepwise catalysis of ATP hydrolysis. As the cleavage happens, the central shaft is pointing to 200°, which was substantiated in their study. Credit: Dr. Tomoko Masaike

Adenosine triphosphate (ATP) is the energy currency of cells. It powers various cellular processes that require energy, including enzymatic reactions. ATP is synthesized with the help of an enzyme complex called F-type ATP synthase. This enzyme complex has a bidirectional functionality, working to synthesize ATP as well as hydrolyzing it, depending on environmental and cellular cues.

ATP synthase consists of two rotating motors—F1 and F0. The F1 subcomplex is mainly composed of α, β, and γ subunits. During the hydrolysis of ATP, the F1-ATPase show rotational motion. Therefore, F1-ATPase is also known as the world’s smallest

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