1e4o: Difference between revisions

Revision as of 00:08, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1e4o.png

Template:STRUCTURE 1e4o

PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTIONPHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION

Template:ABSTRACT PUBMED 10469642

About this StructureAbout this Structure

1E4O is a Single protein structure of sequence from Escherichia coli. 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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OCA

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-'''PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION'''
+===PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION===
-==Overview==
+<!--
-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 resolution; and the 2.1 A resolution ternary complex of MalP with thio-oligosaccharide and phosphate (GSG4-P). The results show a pentasaccharide bound across the catalytic site of MalP with sugars occupying sub-sites -1 to +4. Binding of GSG4 is identical to the natural pentasaccharide, indicating that the inactive thio compound is a close mimic of the natural substrate. The ternary MalP-GSG4-P complex shows the phosphate group poised to attack the glycosidic bond and promote phosphorolysis. In all three complexes the pentasaccharide exhibits an altered conformation across sub-sites -1 and +1, the site of catalysis, from the preferred conformation for alpha(1-4)-linked glucosyl polymers.
+The line below this paragraph, {{ABSTRACT_PUBMED_10469642}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Maltopentaose]]
 [[Category: Phosphorylase mechanism]]
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