Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

Structural changes in glycogen phosphorylase induced by phosphorylation

Nature volume 336, pages 215–221 (1988)Cite this article

Abstract

A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the surface of the dimer. The consequent structural changes at the N- and C-terminal regions lead to strengthened interactions between subunits and alter the binding sites for allosteric effectors and substrates.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Krebs, E. G. in The Enzymes 3rd edn Vol. 17 (eds Boyer, P. D. & Krebs, E. G.) 3–20 (Academic, New York, 1986).

    Google Scholar 

  2. Cohen, P. Eur. J. Biochem. 151, 439–448 (1985).

    CAS  PubMed  Google Scholar 

  3. Krebs, E. B. & Fischer, E. H. Biochem. biophys. Acta. 20, 150–157 (1956).

    CAS  PubMed  Google Scholar 

  4. Graves, D. J. & Wang, J. H. in The Enzymes 3rd edn Vol. 7 (ed. Boyer, P. D.) 435–482 (Academic, New York, 1972).

    Google Scholar 

  5. Fletterick, R. J. & Madsen, N. B. A. Rev. Biochem. 49, 31–61 (1980).

    CAS  Google Scholar 

  6. Dombradi, V. Int. J. Biochem. 13, 125–139 (1981).

    CAS  PubMed  Google Scholar 

  7. Fletterick, R. J. & Sprang, S. R. Acct Chem. Res. 15, 361–369 (1982).

    CAS  Google Scholar 

  8. Madsen, N. B. in The Enzymes 3rd edn Vol. 17 (eds Boyer, P. D. & Krebs, E. G.) 366–394 (Academic, New York, 1986).

    Google Scholar 

  9. Johnson, L. N. et al. in Allosteric Enzymes (ed. Herve, G., CRC in the press).

  10. Metzger, B. E., Glaser, L. & Helmreich, E. Biochemistry 7, 2021–2036 (1968).

    CAS  PubMed  Google Scholar 

  11. Engers, H. D., Shechosky, S. & Madsen, N. B. Can. J. Biochem. 48, 746–754 (1970).

    CAS  PubMed  Google Scholar 

  12. Helmreich, E., Michaelides, M. C. & Cori, C. F. Biochemistry 6, 3695–3710 (1967).

    CAS  PubMed  Google Scholar 

  13. Johnson, L. N., Madsen, N. B., Mosley, J. & Wilson, K. S. J. molec. Biol. 90, 703–717 (1974).

    CAS  PubMed  Google Scholar 

  14. Fletterick, R. J., Sygusch, J., Semple, H., Madsen, N. B. & Johnson, L. N. J. molec. Biol. 103, 1–13 (1976).

    CAS  PubMed  Google Scholar 

  15. Black, W. J. & Wang, J. H. J. biol. Chem. 243, 5892–5898 (1968).

    CAS  PubMed  Google Scholar 

  16. Kasvinsky, P. J., Schechosky, S. & Fletterick, R. J. J. biol. Chem. 253, 9102–9106 (1978).

    CAS  PubMed  Google Scholar 

  17. Fletterick, R. J., Sygusch, J., Semple, H. & Madsen, N. B. J. biol. Chem. 251, 6142–6146 (1976).

    CAS  PubMed  Google Scholar 

  18. Weber, I. T. et al. Nature 274, 433–437 (1978).

    ADS  CAS  PubMed  Google Scholar 

  19. Sprang, S. R. & Fletterick, R. J. J. molec. Biol. 131, 523–551 (1979).

    CAS  PubMed  Google Scholar 

  20. Sansom, M. S. P. et al. J. Mol. Struct. 123, 3–25 (1985).

    Google Scholar 

  21. Sprang, S. R., Goldsmith, E. J., Fletterick, R. J., Withers, S. G. & Madsen, N. B. Biochemistry 21, 5364–5371 (1982).

    CAS  PubMed  Google Scholar 

  22. Sprang, S. R. & Fletterick, R. J. Biophys. J. 32, 175–192 (1980).

    ADS  CAS  PubMed  PubMed Central  Google Scholar 

  23. Hendrickson, W. A. Acta crystallogr. A35, 158–163 (1979).

    ADS  CAS  Google Scholar 

  24. Luzzati, V. Acta crystallogr. 5, 802–810 (1952).

    Google Scholar 

  25. Lee, B. & Richards, F. M. J. molec. Biol. 55, 397–400 (1971).

    Google Scholar 

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

    CAS  PubMed  PubMed Central  Google Scholar 

  27. Stura, E. A. et al. J. molec. Biol. 170, 529–565 (1983).

    CAS  PubMed  Google Scholar 

  28. Kasvinsky, P. J., Madsen, N. B., Sygusch, J. & Fletterick, R. J. J. biol. Chem. 254, 3343–3351 (1978).

    Google Scholar 

  29. Sprang, S. R., Goldsmith, E. & Fletterick, R. J. Science 237, 1012–1019 (1987).

    ADS  CAS  PubMed  Google Scholar 

  30. Oikonomakos, N. G. et al. Biochemistry 26, 8381–8389 (1987).

    CAS  PubMed  Google Scholar 

  31. Graves, D. J., Mann, S. A. S., Philip, G. & Oliveira, R. J. J. biol. chem. 243, 6090–6098 (1968).

    CAS  PubMed  Google Scholar 

  32. Janski, A. M. & Graves, D. J. J. biol. Chem. 254, 4033–4039 (1979).

    CAS  PubMed  Google Scholar 

  33. Gusev, N. B., Hajdu, J. & Friedrich, P. Biochem. biophys. Res. Commun. 90, 70–77 (1979).

    CAS  PubMed  Google Scholar 

  34. Mateo, P. L., Baron, C., Lopez-Mayorga, O., Jimenez, J. S. & Cortijo, M. J. biol. Chem. 259, 9384–9389 (1984).

    CAS  PubMed  Google Scholar 

  35. Kastenschmidt, L. L., Kastenschmidt, J. & Helmreich, W. Biochemistry 1, 4543–4556 (1968).

    Google Scholar 

  36. Vanderbunder, B., Dreyfus, M. & Buc, H. Biochemistry 17, 4153–4160 (1978).

    Google Scholar 

  37. Morgan, H. E. & Parmeggiani, A. J. J. biol. Chem. 239, 2440–2445 (1964).

    CAS  PubMed  Google Scholar 

  38. Melpidou, A. E. & Oikonomakos, N. G. FEBS Lett. 154, 105–110 (1983).

    CAS  PubMed  Google Scholar 

  39. Oikonomakos, N. G. et al. Eur. J. Biochem. 173, 569–579 (1988).

    CAS  PubMed  Google Scholar 

  40. Hajdu, J. et al. EMBO J. 6, 539–545 (1987).

    CAS  PubMed  PubMed Central  Google Scholar 

  41. Madsen, N. B., Kasvinsky, P. J. & Fletterick, R. J. J. biol. Chem. 253, 9097–9101 (1978).

    CAS  PubMed  Google Scholar 

  42. Withers, S. G., Madsen, N. B., Sprang, S. R. & Fletterick, R. J. Biochemistry 21, 4372–5382 (1982).

    Google Scholar 

  43. Krebs, E. G. & Beavo, J. A. A. Rev. Biochem. 48, 923–959 (1979).

    CAS  Google Scholar 

  44. Cohen, P. Proc. R. Soc. Lond. B234, 115–144 (1988).

    ADS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry and University of Texas Southwestern Medical Centre, Dallas, Texas, 75235-9050, USA

    S. R. Sprang & E. J. Goldsmith

  2. Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    K. R. Acharya, D. I. Stuart, K. Varvill & L. N. Johnson

  3. Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143, USA

    R. J. Fletterick

  4. Department of Biochemistry, University of Alberta, Edmonton, Canada, T6G 2H7

    N. B. Madsen

Authors
  1. S. R. Sprang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. K. R. Acharya
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. E. J. Goldsmith
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. D. I. Stuart
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. K. Varvill
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. R. J. Fletterick
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. N. B. Madsen
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. L. N. Johnson
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sprang, S., Acharya, K., Goldsmith, E. et al. Structural changes in glycogen phosphorylase induced by phosphorylation. Nature 336, 215–221 (1988). https://doi.org/10.1038/336215a0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/336215a0

This article is cited by

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.

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing