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

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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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  1. 1

    Yount, R. G., Ojala, D., and Babcock, D., Biochemistry, 10, 2490–2496 (1971).

  2. 2

    Marston, S. B., Rodger, C. D., and Tregear, R. T., J. molec. Biol., 104, 263–276 (1976).

  3. 3

    Barrington Leigh, J., et al., Cold Spring Harb. Symp. quant. Biol., 37, 443–447 (1972).

  4. 4

    Goody, R. S., Holmes, K. C., Mannherz, H. G., Barrington Leigh, J., and Rosenbaum, G., Biophys. J., 15, 687–705 (1975).

  5. 5

    Beinbreck, G., Kuhn, H. J., Herzig, J. W., and Rüegg, J. C., Cytobiologie, 12, 385–396 (1976).

  6. 6

    Reedy, M. K., Am. Zool., 7, 465–481 (1967).

  7. 7

    Barrington Leigh, J., and Rosenbaum, G., A. Rev. Biophys. Bioengng., 5, 239–270 (1976).

  8. 8

    Barrington Leigh, J., and Rosenbaum, G., J. appl. Crystallogr., 7, 117–121 (1974).

  9. 9

    Gabriel, A., and Dupont, Y., Rev. Sci. Instrum., 43, 1600–1602 (1972).

  10. 10

    Miller, A., and Tregear, R. T., J. molec. Biol., 70, 85–104 (1972).

  11. 11

    Marston, S. B., Biochim. biophys. Acta, 305, 397–412 (1973).

  12. 12

    Holmes, K. C., et al., in Molecular Basis of Motility (edit. by Heilmeyer, L. M. G., Rüegg, J. C. and Wieland, Th.), 26–41 (Springer, Heidelberg, 1976).

  13. 13

    Beinbrech, G., Kuhn, H. J., and Rüegg, J. C., Experientia, 28, 513–515 (1972).

  14. 14

    White, D. C. S., J. Physiol., Lond., 208, 583–605 (1970).

  15. 15

    Rodger, C. D., and Tregear, R. T., J. molec. Biol., 86, 495–497 (1974).

  16. 16

    Lymn, R. W., J. molec. Biol., 99, 567–582 (1975).

  17. 17

    Haselgrove, J. C., and Huxley, H. E., J. molec. Biol., 77, 549–568 (1973).

  18. 18

    Wilkinson, G. N., Biochem. J., 80, 324–332 (1961).

  19. 19

    Armitage, P. M., Tregear, R. T., and Miller, A., J. molec. Biol., 92, 39–53 (1975).

  20. 20

    Feldhaus, P., Fröhlich, T., Goody, R. S., Isakov, M., and Schirmer, R. H., Eur. J. Biochem., 57, 197–204 (1975).

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