Abstract
High resolution studies on the crystal structure of glycogen phosphorylase b have identified the catalytic site to which the substrate glucose-1-phosphate binds strongly with some local conformational changes. The site is situated 8 Å (phosphate-to-phosphate distance) from pyridoxal phosphate, an essential cofactor of all glycogen phosphorylases. The catalytic site is 33 Å from the site in the N-terminal portion of the molecule to which adenine nucleotides bind. In contrast to phosphorylase a (the active form of the enzyme which is phosphorylated at Ser 14), the positions of the first 19 residues of phosphorylase b are not well defined.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Cori, G. T. & Cori, C. F. J. biol. Chem. 135, 733–756 (1940).
Graves, D. J. & Wang, J. H. in The Enzymes, 3rd edn, Vol. 7, (ed. Boyer, P. D.) 435–482 (Academic, New York, 1972).
Eagles, P. A. M., Iqbal, M., Johnson, L. N., Mosley, J. & Wilson, K. S. J. molec. Biol. 71, 803–806 (1972).
Johnson, L. N., Madsen, N. B., Mosley, J. & Wilson, K. S. J. molec. Biol. 90, 703–717 (1974).
Johnson, L. N., Weber, I. T., Wild, D. L., Wilson, K. S. & Yeates, D. G. R. Proc. 11th FEBS Mtg., Copenhagen, 1977, Vol. 42 (ed. Esmann, V.) 185–194 (Pergamon, Oxford, 1978).
Fletterick, R. J., Sygusch, J., Murray, N., Madsen, N. B. & Johnson, L. N. J. molec. Biol. 103, 1–13 (1976).
Fletterick, R. J., Sygusch, J., Semple, M. & Madsen, N. B. J. biol. Chem. 251, 6142–6146 (1976).
Sygusch, J., Madsen, N. B., Kasvinsky, P. J. & Fletterick, R. J. Proc. natn Acad. Sci. U.S.A. 74, 4757–4761 (1977).
Black, W. I. & Wang, J. H. J. biol. Chem. 243, 5892–5898 (1968).
Johnson, L. N., Weber, I. T., Wild, D. L., Wilson, K. S. & Yeates, D. G. R. J. molec. Biol. 118, 579–591 (1978).
Titani, K. et al. Proc. natn. Acad. Sci. U.S.A. 74, 4762–4766 (1977).
Battell, M. L., Sarkadas, C. G., Smillie, L. B. & Madsen, N. B. J. biol. Chem. 243, 6202–6209 (1968).
Akramovic-Kicic, O., Smillie, L. B. & Madsen, N. B. J. biol. Chem. 245, 1358–1365 (1970).
Li, E. G. Y., Fletterick, R. J., Sygusch, J. & Madsen, N. B. Can. J. Biochem. 55, 465–473 (1977).
Richardson, J. S. Nature 268, 495–500 (1977).
Rossmann, M. C., Moras, D. & Olsen, K. W. Nature 250, 194–199 (1974).
Stellwagen, E., Cass, R., Thompson, S. T. & Woody, M. Nature 257, 716–718 (1975).
Feldman, K. & Hull, W. E. Proc. natn. Acad. Sci. U.S.A. 74, 856–860 (1977).
Feldman, K., Hörl, M., Klein, H. W. & Helmreich, E. J. M. Proc. 11th FEBS Mtg., Copenhagen, 1977, Vol. 42 (ed. Esmann, V.) 205–218 (Pergamon, Oxford, 1978).
Graves, D. J., Parrish, R. F., Ulring, R. J. & Korytnyk, W. Proc. 11th FEBS Mtg., Copenhagen, 1977, Vol. 42 (ed. Esmann, V.) 195–204 (Pergamon, Oxford, 1978).
Fischer, E. H., Kent, A. B., Snyder, E. R. & Krebs, E. G. J. Am. chem. Soc. 80, 2906–2907 (1958).
Shaltiel, S. & Cortijo, M. Biochem. biophys. Res. Commun. 41, 594–600 (1970).
Jones, D. C. & Cowgill, R. W. Biochemistry 10, 4276–4282 (1971).
Honikel, K. O. & Madsen, N. B. Can. J. Biochem. 51, 344–356 (1973).
Beevers, C. A. & Maconochie, G. H. Acta crystallogr. 18, 232–236 (1965).
Barry, C. D. & North, A. C. T. Cold Spring Harb. Symp. quant. Biol. 36, 577–584 (1971).
Sundararajan, P. R. & Rao, V. S. R. Biopolymers 8, 313–323 (1969).
Hybl, A., Rundle, R. E. & Williams, D. E. J. Am. chem. Soc. 87, 2779–2788 (1965).
Rees, D. A. & Smith, P. J. C. JCS Perkin II, 836–840 (1975).
Rees, D. A. Polysaccharide Shapes (Chapman and Hall, London, 1977).
McCarty, T. J., Tu, J-I. & Graves, D. J. J. biol. Chem. 250, 4980–4985 (1975).
Fehlhammer, H., Bode, W. & Huber, R. J. molec. Biol. 111, 415–437 (1977).
Fischer, E. H., Graves, D. J., Crittenden, E. R. S. & Krebs, E. G. J. biol. Chem. 234, 1698–1704 (1959).
Graves, D. H., Mann, S. A. S., Philip, G. & Oliveira, R. J. J. biol. Chem. 243, 6090–6098 (1968).
Feldman, K., Zeisel, H. J. & Helmreich, E. J. M. Eur. J. Biochem 65, 285–291 (1976).
Pai, E. F., Sachsenheimer, W., Schirma, R. M. & Schulz, G. E. J. molec. Biol. 114, 37–45 (1977).
Kasvinsky, P. J., Madsen, N. B., Fletterick, R. J. & Sygusch, J. J. biol. Chem. 253, 1290–1296 (1978).
Wang, J. H., Kwok, S-C., Wirch, E. & Susuki, I. Biochem. biophys. Res. Commun. 40, 1340–1347 (1965).
Meyer, F., Heilmeyer, L. M. G., Haschke, R. H. & Fischer, E. H. J. biol. Chem. 245, 6642–6648 (1970).
Anderson, R. A. & Graves, D. J. Biochemistry 12, 1895–1900 (1973).
Anderson, R. A., Parrish, R. F. & Graves, D. J. Biochemistry 12, 1901–1906 (1973).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Weber, I., Johnson, L., Wilson, K. et al. Crystallographic studies on the activity of glycogen phosphorylase b. Nature 274, 433–437 (1978). https://doi.org/10.1038/274433a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/274433a0
This article is cited by
-
Intersubunit communication in glycogen phosphorylase influences substrate recognition at the catalytic sites
Amino Acids (2024)
-
5-Aminolevulinate synthase and the first step of heme biosynthesis
Journal of Bioenergetics and Biomembranes (1995)
-
The allosteric transition of glycogen phosphorylase
Nature (1989)
-
Glycogen phosphorylase: A multifaceted enzyme
Carlsberg Research Communications (1989)
-
Structural changes in glycogen phosphorylase induced by phosphorylation
Nature (1988)
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.
