1u1g: Difference between revisions
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|PDB= 1u1g |SIZE=350|CAPTION= <scene name='initialview01'>1u1g</scene>, resolution 1.95Å | |PDB= 1u1g |SIZE=350|CAPTION= <scene name='initialview01'>1u1g</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=BBB:1-((2-HYDROXYETHOXY)METHYL)-5-(3-(BENZYLOXY)BENZYL)-6-HYDROXYPYRIMIDINE-2,4(1H,3H)-DIONE'>BBB</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] </span> | ||
|GENE= UDP, B3831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= UDP, B3831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1tgw|1TGW]], [[1tgy|1TGY]], [[1tgv|1TGV]], [[1u1c|1U1C]], [[1u1d|1U1D]], [[1u1e|1U1E]], [[1u1f|1U1F]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u1g OCA], [http://www.ebi.ac.uk/pdbsum/1u1g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u1g RCSB]</span> | |||
}} | }} | ||
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[[Category: Ealick, S E.]] | [[Category: Ealick, S E.]] | ||
[[Category: Settembre, E C.]] | [[Category: Settembre, E C.]] | ||
[[Category: | [[Category: 5-(m-(benzyloxy)benzyl)acyclouridine]] | ||
[[Category: | [[Category: bbba]] | ||
[[Category: pyrimidine nucleoside phosphorylase | [[Category: pyrimidine nucleoside phosphorylase]] | ||
[[Category: udp]] | |||
[[Category: uridine salvage]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:03 2008'' | ||
Revision as of 00:04, 31 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | UDP, B3831 (Escherichia coli) | ||||||
| Activity: | Uridine phosphorylase, with EC number 2.4.2.3 | ||||||
| Related: | 1TGW, 1TGY, 1TGV, 1U1C, 1U1D, 1U1E, 1U1F
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of E. coli uridine phosphorylase complexed to 5-(m-(benzyloxy)benzyl)barbituric acid (BBBA)
OverviewOverview
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.
About this StructureAbout this Structure
1U1G 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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