Abstract
WE have attempted to establish a correlation between the binding of an ATP analogue, β, γ-imido-ATP (hereafter termed imido-ATP), and a structural change induced in muscle in the presence of this analogue. Imido-ATP binds tightly at the enzymatic site of myosin, but is not hydrolysed there1. When applied to glycerol-extracted muscle, it binds to the myosin in situ without causing the muscle to relax—that is, a ternary actin–myosin–nucleotide complex is formed2. Muscle fibres in this condition have the same mechanical stiffness as in rigor, but their zero tension point is displaced to a slightly greater muscle length, and both X-ray diffraction and electron microscopy indicate that the conformation of the attached myosin has altered, as if the head was rotated relative to the actin2–5.
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GOODY, R., LEIGH, J., MANNHERZ, H. et al. X-ray titration of binding of β, γ-imido-ATP to myosin in insect flight muscle. Nature 262, 613–615 (1976). https://doi.org/10.1038/262613a0
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DOI: https://doi.org/10.1038/262613a0
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