The structural coupling between ATPase activation and recovery stroke in the myosin II motor.
Before the myosin motor head can perform the next power stroke, it undergoes a large conformational transition in which the converter domain, bearing the lever arm, rotates approximately 65 degrees . Simultaneous with this "recovery stroke," myosin activates its ATPase function by closing the Switch-2 loop over the bound ATP. This coupling between the motions of the converter domain and of the 40 A-distant Switch-2 loop is essential to avoid unproductive ATP hydrolysis. The coupling mechanism is determined here by finding a series of optimized intermediates between crystallographic end structures of the recovery stroke (Dictyostelium discoideum), yielding movies of the transition at atomic detail. The successive formation of two hydrogen bonds by the Switch-2 loop is correlated with the successive see-saw motions of the relay and SH1 helices that hold the converter domain. SH1 helix and Switch-2 loop communicate via a highly conserved loop that wedges against the SH1-helix upon Switch-2 closing.
Koppole
Sampath
S
Computational Biochemistry, Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, 69120, Heidelberg, Germany.
Smith
Jeremy C
JC
Fischer
Stefan
S
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004023:Dictyostelium / Q000502:physiology*; D004789:Enzyme Activation; D008958:Models, Molecular; D009038:Motion; D024462:Myosin Type II / Q000737:chemistry* / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D000251:Adenosine Triphosphatases; D024462:Myosin Type II