Key result
Crystal structures of scallop myosin S1 reveal an unwound SH1 helix in weak actin-binding states, which acts as a clutch controlling the transmission of torque to the lever arm.
Population
Scallop myosin S1 complexed with ADP.BeF(x) and ATP analogs
Design
Preclinical
Authors
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No immediate clinical implications; leaves open relevance of this clutch mechanism to human cardiac myosin function.
Structural analysis of scallop myosin S1 reveals the mechanical roles of motor parts during the contractile cycle, suggesting how strong actin binding triggers the power stroke and product release.
Himmel et al. (2002) studied this question. Crystal structures of scallop myosin S1 reveal an unwound SH1 helix in weak actin-binding states, which acts as a clutch controlling the transmission of torque to the lever arm.
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