PMID:9145112

Citation	O'Reilly, M, Watson, KA, Schinzel, R, Palm, D and Johnson, LN (1997) Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase. Nat. Struct. Biol. 4:405-12
Abstract	The crystal structure of E. coli maltodextrin phosphorylase co-crystallized with an oligosaccharide has been solved at 3.0 A resolution, providing the first structure of an oligosaccharide bound at the catalytic site of an alpha-glucan phosphorylase. An induced fit mechanism brings together two domains across the catalytic site tunnel. A stacking interaction between the glucosyl residue and the aromatic group of a tyrosine residue at a sub-site remote (8 A) from the catalytic site provides a key element in substrate recognition; mutation of this residue to Ala decreases the Kcat/Km by 10(4). Extrapolation of the results to substrate binding across the site of attack by phosphorolysis indicates a likely alteration in the glycosidic torsion angles from their preferred values, an alteration that appears to be important for the catalytic mechanism.
Links	PubMed
Keywords	Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Glucans/chemistry; Glucans/metabolism; Glucosyltransferases/chemistry; Glucosyltransferases/metabolism; Kinetics; Models, Molecular; Oligosaccharides/chemistry; Oligosaccharides/metabolism; Protein Binding; Protein Conformation; Tyrosine/physiology
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