This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1u1c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u1c.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1u1c.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u1c| PDB=1u1c | SCENE= }}
{{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==
==About this Structure==
Line 30: Line 34:
[[Category: Pyrimidine nucleoside phosphorylase]]
[[Category: Pyrimidine nucleoside phosphorylase]]
[[Category: Uridine salvage]]
[[Category: Uridine salvage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:37:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:58:22 2008''

Revision as of 02:58, 29 July 2008

Image:1u1c.png

Template:STRUCTURE 1u1c

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

Template:ABSTRACT PUBMED 15983408

About this Structure

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

Reference

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

Page seeded by OCA on Tue Jul 29 05:58:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u1c"
Personal tools