Motor proteins require energy in the form of ATP. ATP hydrolysis results in a conformational change that allows the protein to move along microtubular tracks (pathways). What structural component of the motor protein contains the ATP binding site and, therefore, changes shape to enable movement?

The correct answer will be - the head globular domain of the motor protein.

Explanation:

Motor proteins are a class of proteins which can move along the cytoskeletal system of the cell using a mechano-chemical mechanism which involves conformational change, filament binding and releasing.

The kinesin and myosin are two important motor proteins which move along the actin filaments by converting the chemical energy of the ATP into motion.

The structure of motor molecules contains two globular head domains which bind ATP and ATPase enzyme break down the ATP releasing energy utilized by the motor protein to move.

Thus, the head domain of the motor protein enables movement.