1e4o: Difference between revisions
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PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION
OverviewOverview
Phosphorylases are key enzymes of carbohydrate metabolism. Structural, studies have provided explanations for almost all features of control and, substrate recognition of phosphorylase but one question remains, unanswered. How does phosphorylase recognize and cleave an oligosaccharide, substrate? To answer this question we turned to the Escherichia coli, maltodextrin phosphorylase (MalP), a non-regulatory phosphorylase that, shares similar kinetic and catalytic properties with the mammalian, glycogen phosphorylase. The crystal structures of three, MalP-oligosaccharide complexes are reported: the binary complex of MalP, with the natural substrate, maltopentaose (G5); the binary complex with, the thio-oligosaccharide, 4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose, (GSG4), both at 2.9 A ... [(full description)]
About this StructureAbout this Structure
1E4O is a [Single protein] structure of sequence from [Escherichia coli] with PLP as [ligand]. Active as [Phosphorylase], with EC number [2.4.1.1]. Structure known Active Sites: PLA and PLB. Full crystallographic information is available from [OCA].
ReferenceReference
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question., Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN, EMBO J. 1999 Sep 1;18(17):4619-32. PMID:10469642
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