Article | Published:

The allosteric transition of glycogen phosphorylase

Nature volume 340, pages 609616 (24 August 1989) | Download Citation

Subjects

Abstract

The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 Å resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary con-formational change that switches these two helices into the R-state conformation.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    & Proc. Soc. exp. Biol. Med. 34, 202–205 (1936).

  2. 2.

    & in The Enzymes, 3rd edn Vol. 7 (ed. Boyer, P.) 435–482 (Academic Press, New York, 1972).

  3. 3.

    , & J. molec. Biol. 12, 88–118 (1965).

  4. 4.

    & J. biol. Chem. 243, 5892–5898 (1968).

  5. 5.

    & Proc. natn. Acad. Sci. U.S.A. 51, 131–138 (1964).

  6. 6.

    , & Proc. natn. Acad. Sci. U.S.A. 57, 994–1001 (1967).

  7. 7.

    & J. Biochemistry 9, 660–671 (1970).

  8. 8.

    , & Biochemistry 4, 2296–2301 (1965).

  9. 9.

    , , & J. biol. Chem. 245, 6642–6663 (1970).

  10. 10.

    & J. Cell Biol. 38, 130–150 (1968).

  11. 11.

    & Curr. Topics cell Regul. 10, 89–160 (1976).

  12. 12.

    , , & J. molec. Biol. 90, 703–717 (1974).

  13. 13.

    , , , & J. molec. Biol. 103, 1–13 (1976).

  14. 14.

    , & J. biol. Chem. 253, 9102–9106 (1978).

  15. 15.

    et al. Nature 536, 215–221 (1988).

  16. 16.

    et al. J. molec. Structure 123, 3–25 (1985).

  17. 17.

    , & in Metabolic Interconversion of Enzymes (eds. Wieland, O., Helmreich, E. & Holzer, H.) 448 (Springer, Berlin, 1972).

  18. 18.

    , , , & FEBS Lett. 21, 229–232 (1972).

  19. 19.

    & Biophys. Struct. Mechanism 2, 43–59 (1976).

  20. 20.

    & Biochem. biophys. Res. Commun. 33, 49–54 (1968).

  21. 21.

    , & Biochem. biophys. Res. Commun. 90, 234–239 (1978).

  22. 22.

    J. appl. Crystallogr. 21, 274–278 (1988).

  23. 23.

    & Acta crystallogr. 23, 544–548 (1967).

  24. 24.

    , , & Acta crystallogr. A33, 800–804 (1977).

  25. 25.

    , & Acta crystallogr. A45, 50–61 (1989).

  26. 26.

    et al. Biochemistry 26, 8381–8389 (1987).

  27. 27.

    et al. in Current Topics in Microbiology and Immunology 139, 81–134 (eds Clark, A. E. & Wilson, I. A) (Springer, Berlin & Heidelberg, 1988).

  28. 28.

    Acta crystallogr. A35, 158–173 (1979).

  29. 29.

    A. Rev. Biochem. 53, 537–572 (1984).

  30. 30.

    et al. in Allosteric Enzymes (ed. Herve, G.) (CRC, Boca Ratn, Florida, in the press).

  31. 31.

    et al. EMBO J. 6, 539–546 (1987).

  32. 32.

    et al. Biochem. J. 218, 45–60 (1984).

  33. 33.

    , & Biochemistry 7, 4543–4556 (1968).

  34. 34.

    , & in Chemical and Biological Aspects of Vitamin B6 Catalysis Part A (ed. Evangelopoulos, A. E.) 147–160 (Liss, New York, 1984).

  35. 35.

    , , , & Biochemistry 23, 5862–5873 (1984).

  36. 36.

    , & Biochemistry 19, 3634–3642 (1980).

  37. 37.

    & Eur. J. Biochem. 133, 509–513 (1983).

  38. 38.

    , & Biochemistry 16, 4824–4831 (1977).

  39. 39.

    & Proc. natn. Acad. Sci. U.S.A. 74, 836–860 (1977).

  40. 40.

    & Angew. Chem. Int. Ed. Engl. 19, 441–455 (1980).

  41. 41.

    Proc. natn. Acad. Sci. U.S.A. 44, 98–99 (1958).

  42. 42.

    , Biochem. biophys. Res. Commun. 28, 59–64 (1967).

  43. 43.

    & J. molec. Biol. 174, 175–191 (1984).

  44. 44.

    , , & Nature 302, 500–505 (1983).

  45. 45.

    & in The Rotation Method in Crystallography (eds Arndt, U. W. & Wonacott, A. J.) 139–152 (North-Holland, Amsterdam, 1977).

  46. 46.

    thesis, Univ. Oxford (1988).

  47. 47.

    et al. Nature 274, 433–437 (1978).

  48. 48.

    , & Science 237, 1012–1019 (1987).

Download references

Author information

Affiliations

  1. Laboratory of Molecular Biophysics, University of Oxford, The Rex Richards Building, South Parks Road, Oxford 0X1 3QU, UK

    • D. Barford
    •  & L. N. Johnson

Authors

  1. Search for D. Barford in:

  2. Search for L. N. Johnson in:

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/340609a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.