Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 29 November 1991:
Vol. 254. no. 5036, pp. 1367 - 1371
DOI: 10.1126/science.1962195
Prev | Table of Contents | Next

Articles

Science, Vol 254, Issue 5036, 1367-1371
Copyright © 1991 by American Association for the Advancement of Science

articles

Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate

Sprang SR, SG Withers, EJ Goldsmith, RJ Fletterick, and NB Madsen

Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.

The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Crystal Structures of the Open and Catalytically Competent Closed Conformation of Escherichia coli Glycogen Synthase.
F. Sheng, X. Jia, A. Yep, J. Preiss, and J. H. Geiger (2009)
J. Biol. Chem. 284, 17796-17807
   Abstract »    Full Text »    PDF »
Activation of 4-{alpha}-Glucanotransferase Activity of Porcine Liver Glycogen Debranching Enzyme with Cyclodextrins.
Y. Watanabe, Y. Makino, and K. Omichi (2006)
J. Biochem. 140, 135-140
   Abstract »    Full Text »    PDF »
Thermodynamic Characterization of 5'-AMP Binding to Bovine Liver Glycogen Phosphorylase a.
L. Garcia-Fuentes, A. Camara-Artigas, O. Lopez-Mayorga, and C. Baron (1996)
J. Biol. Chem. 271, 27569-27574
   Abstract »    Full Text »    PDF »
Chimeric Muscle and Brain Glycogen Phosphorylases Define Protein Domains Governing Isozyme-specific Responses to Allosteric Activation.
M. M. Crerar, O. Karlsson, R. J. Fletterick, and P. K. Hwang (1995)
J. Biol. Chem. 270, 13748-13756
   Abstract »    Full Text »    PDF »
Flavopiridol Inhibits Glycogen Phosphorylase by Binding at the Inhibitor Site.
N. G. Oikonomakos, J. B. Schnier, S. E. Zographos, V. T. Skamnaki, K. E. Tsitsanou, and L. N. Johnson (2000)
J. Biol. Chem. 275, 34566-34573
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)