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X-ray titration of binding of β, γ-imido-ATP to myosin in insect flight muscle

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Barrington Leigh,  J.
Max Planck Institute for Medical Research, Max Planck Society;

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Mannherz,  Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Rosenbaum,  G.
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Goody, R. S., Barrington Leigh, J., Mannherz, H. G., Rosenbaum, G., & Tregear, R. (1976). X-ray titration of binding of β, γ-imido-ATP to myosin in insect flight muscle. Nature, 262(5569), 613-615. doi:10.1038/262613a0.


Cite as: http://hdl.handle.net/21.11116/0000-0002-ACF9-4
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.