The structure of myosin and its role in energy transduction in muscle.
The present understanding of the relationship between the structure of the myosin ATPase and its role in force production for muscle contraction is reviewed. Emphasis is placed on structural transitions in myosin that occur during ATP hydrolysis which may be correlated with force production. Although detailed structural information is presently lacking, numerous spectroscopic and kinetic experiments have indicated that myosin exists in two structural states for each chemical intermediate in the hydrolysis of ATP. Models are discussed which view a transition between these two states as the energy transduction "event" (i.e., force production).
D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002151:Calorimetry; D004734:Energy Metabolism; D007700:Kinetics; D008954:Models, Biological; D008961:Models, Structural; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism
D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins