Catalytic strategy used by the myosin motor to hydrolyze ATP

Significance

Biomolecular motor proteins like myosin generate mechanical force from the chemical energy of ATP. Like gas engines, they have different parts (protein domains) that run through a well-defined cycle of motions, consuming one ATP per cycle. Because ATP is very stable, motor proteins catalyze its breakdown (hydrolysis). The catalytic mechanism is at the core of understanding how these motors work, because the activation of the catalytic ATPase-function coordinates the motion of the different domains. Identifying which protein groups are essential for catalysis allows one to understand how the precise coupling between ATPase activation and mechanical motion is achieved. Moreover, ATPases are involved in most biochemical processes and are expected to have a catalytic strategy very similar to the one reported here.