Key result
Myosin V is a highly efficient processive motor that walks in strides averaging approximately 36 nm, with each step coupled to a single ATP hydrolysis.
Summarizes recent findings on the mechanics of myosin V, highlighting its 36 nm step size and highly efficient processive motor capabilities.
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No immediate clinical implications in cardiology; leaves open extension of motor kinetics to cardiovascular cell models.
Recent experiments, drawing upon single-molecule, solution kinetic and structural techniques, have clarified our mechanistic understanding of class V myosins. The findings of the past two years can be summarized as follows: (1) Myosin V is a highly efficient processive motor, surpassing even conventional kinesin in the distance that individual molecules can traverse. (2) The kinetic scheme underlying ATP turnover resembles those of myosins I and II but with rate constants tuned to favor strong binding to actin. ADP release precedes dissociation from actin and is rate-limiting in the cycle. (3) Myosin V walks in strides averaging approximately 36 nm, the long pitch pseudo-repeat of the actin helix, each step coupled to a single ATP hydrolysis. Such a unitary displacement, the largest molecular step size measured to date, is required for a processive myosin motor to follow a linear trajectory along a helical actin track.
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Amit Mehta (2001) reported a review. Class V myosins was evaluated. Myosin V is a highly efficient processive motor that walks in strides averaging approximately 36 nm, with each step coupled to a single ATP hydrolysis.
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