1U1C
Structure of E. coli uridine phosphorylase complexed to 5-benzylacyclouridine (BAU)
Summary for 1U1C
| Entry DOI | 10.2210/pdb1u1c/pdb |
| Related | 1TGV 1TGW 1TGY 1U1D 1U1E 1U1F 1U1G |
| Descriptor | Uridine phosphorylase, PHOSPHATE ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | pyrimidine nucleoside phosphorylase; uridine salvage; benzylacyclouridine; bau, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 167172.85 |
| Authors | Bu, W.,Settembre, E.C.,Ealick, S.E. (deposition date: 2004-07-15, release date: 2005-07-05, Last modification date: 2024-02-14) |
| Primary citation | Bu, W.,Settembre, E.C.,el Kouni, M.H.,Ealick, S.E. Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines. Acta Crystallogr.,Sect.D, 61:863-872, 2005 Cited by PubMed Abstract: 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. PubMed: 15983408DOI: 10.1107/S0907444905007882 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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