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lüll The structure of the rigor complex and its implications for the power stroke Holmes KC; Schroder RR; Sweeney HL; Houdusse APhilos Trans R Soc Lond B Biol Sci 2004[Dec]; 359 (1452): 1819-28Decorated actin provides a model system for studying the strong interaction between actin and myosin. Cryo-energy-filter electron microscopy has recently yielded a 14 A resolution map of rabbit skeletal actin decorated with chicken skeletal S1. The crystal structure of the cross-bridge from skeletal chicken myosin could not be fitted into the three-dimensional electron microscope map without some deformation. However, a newly published structure of the nucleotide-free myosin V cross-bridge, which is apparently already in the strong binding form, can be fitted into the three-dimensional reconstruction without distortion. This supports the notion that nucleotide-free myosin V is an excellent model for strongly bound myosin and allows us to describe the actin-myosin interface. In myosin V the switch 2 element is closed although the lever arm is down (post-power stroke). Therefore, it appears likely that switch 2 does not open very much during the power stroke. The myosin V structure also differs from the chicken skeletal myosin structure in the nucleotide-binding site and the degree of bending of the backbone beta-sheet. These suggest a mechanism for the control of the power stroke by strong actin binding.|*Models, Biological[MESH]|*Models, Molecular[MESH]|Actins/*physiology[MESH]|Animals[MESH]|Biomechanical Phenomena[MESH]|Muscle Contraction/*physiology[MESH]|Muscle, Skeletal/*physiology[MESH]|Myosins/*physiology[MESH]|Protein Conformation[MESH] |