1u1c: Difference between revisions

Revision as of 05:58, 29 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:1u1c.png

Template:STRUCTURE 1u1c

Structure of E. coli uridine phosphorylase complexed to 5-benzylacyclouridine (BAU)Structure of E. coli uridine phosphorylase complexed to 5-benzylacyclouridine (BAU)

Template:ABSTRACT PUBMED 15983408

About this StructureAbout this Structure

1U1C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines., Bu W, Settembre EC, el Kouni MH, Ealick SE, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):863-72. Epub 2005, Jun 24. PMID:15983408

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1u1c|  PDB=1u1c  |  SCENE=  }}
-'''Structure of E. coli uridine phosphorylase complexed to 5-benzylacyclouridine (BAU)'''
+===Structure of E. coli uridine phosphorylase complexed to 5-benzylacyclouridine (BAU)===
-==Overview==
+<!--
-Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uridine to uracil and ribose 1-phosphate and is a key enzyme in the pyrimidine-salvage pathway. Escherichia coli UP is structurally homologous to E. coli purine nucleoside phosphorylase and other members of the type I family of nucleoside phosphorylases. The structures of 5-benzylacyclouridine, 5-phenylthioacyclouridine, 5-phenylselenenylacyclouridine, 5-m-benzyloxybenzyl acyclouridine and 5-m-benzyloxybenzyl barbituric acid acyclonucleoside bound to the active site of E. coli UP have been determined, with resolutions ranging from 1.95 to 2.3 A. For all five complexes the acyclo sugar moiety binds to the active site in a conformation that mimics the ribose ring of the natural substrates. Surprisingly, the terminal hydroxyl group occupies the position of the nonessential 5'-hydroxyl substituent of the substrate rather than the 3'-hydroxyl group, which is normally required for catalytic activity. Until recently, inhibitors of UP were designed with limited structural knowledge of the active-site residues. These structures explain the basis of inhibition for this series of acyclouridine analogs and suggest possible additional avenues for future drug-design efforts. Furthermore, the studies can be extended to design inhibitors of human UP, for which no X-ray structure is available.
+The line below this paragraph, {{ABSTRACT_PUBMED_15983408}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15983408 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15983408}}
 ==About this Structure==
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 [[Category: Pyrimidine nucleoside phosphorylase]]
 [[Category: Uridine salvage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:37:52 2008''
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