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Science 28 August 1987:
Vol. 237. no. 4818, pp. 1012 - 1019
DOI: 10.1126/science.3616621
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Articles

Science, Vol 237, Issue 4818, 1012-1019
Copyright © 1987 by American Association for the Advancement of Science

articles

Structure of the nucleotide activation switch in glycogen phosphorylase a

S Sprang, E Goldsmith, and R Fletterick

Adenosine monophosphate is required for the activation of glycogen phosphorylase b and for release of the inhibition of phosphorylase a by glucose. Two molecules of adenosine monophosphate (AMP) bind to symmetry related sites at the subunit interface of the phosphorylase dimer. Adenosine triphosphate (ATP) binds to the same site, but does not promote catalytic activity. The structure of glucose-inhibited phosphorylase a bound to AMP and also of the complex formed with glucose and ATP is described. Crystallographic refinement of these complexes reveals that structural changes are associated with AMP but not ATP binding. The origin of these effects can be traced to different effector binding modes exhibited by AMP and ATP, respectively. The conformational changes associated with AMP binding traverse multiple paths in the enzyme and link the effector and catalytic sites.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Role of the Active Site Gate of Glycogen Phosphorylase in Allosteric Inhibition and Substrate Binding.
J. L. Buchbinder and R. J. Fletterick (1996)
J. Biol. Chem. 271, 22305-22309
   Abstract »    Full Text »    PDF »
Mechanism of Regulation in Yeast Glycogen Phosphorylase.
K. Lin, P. K. Hwang, and R. J. Fletterick (1995)
J. Biol. Chem. 270, 26833-26839
   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 »
Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate.
Sprang SR, S. Withers, E. Goldsmith, R. Fletterick, and N. Madsen (1991)
Science 254, 1367-1371
   Abstract »    PDF »
Domain separation in the activation of glycogen phosphorylase a.
E. Goldsmith, Sprang SR, R Hamlin, N. Xuong, and R. Fletterick (1989)
Science 245, 528-532
   Abstract »    PDF »


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