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Science 4 August 1989:
Vol. 245. no. 4917, pp. 528 - 532
DOI: 10.1126/science.2756432
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Articles

Science, Vol 245, Issue 4917, 528-532
Copyright © 1989 by American Association for the Advancement of Science

articles

Domain separation in the activation of glycogen phosphorylase a

EJ Goldsmith, Sprang SR, R Hamlin, NH Xuong, and RJ Fletterick

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.

The crystal structure of glycogen phosphorylase a complexed with its substrates, orthophosphate and maltopentaose, has been determined and refined at a resolution of 2.8 angstroms. With oligosaccaride bound at the glycogen storage site, the phosphate ion binds at the catalytic site and causes the regulatory and catalytic domains to separate with the loss of stabilizing interactions between them. Homotropic cooperativity between the active sites of the allosteric dimer results from rearrangements in isologous contacts between symmetry-related helices in the subunit interface. The conformational changes in the core of the interface are correlated with those observed on covalent activation by phosphorylation at Ser14 (phosphorylase b----a).


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Crystal Structures of a Multifunctional Triterpene/Flavonoid Glycosyltransferase from Medicago truncatula.
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Endogenous effectors of human liver glycogen phosphorylase modulate effects of indole-site inhibitors.
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Am J Physiol Endocrinol Metab 289, E366-E372
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Role of the Active Site Gate of Glycogen Phosphorylase in Allosteric Inhibition and Substrate Binding.
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Chimeric Muscle and Brain Glycogen Phosphorylases Define Protein Domains Governing Isozyme-specific Responses to Allosteric Activation.
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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
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Regulation of an enzyme by phosphorylation at the active site.
J. Hurley, A. Dean, J. Sohl, D. Koshland Jr, and R. Stroud (1990)
Science 249, 1012-1016
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Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase.
A. Dean and D. Koshland Jr (1990)
Science 249, 1044-1046
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