4E1V
X-RAY Structure of the Uridine Phosphorylase from Salmonella Typhimurium in Complex with 5-Fluorouracil at 2.15 A Resolution
Replaces: 3NSRSummary for 4E1V
| Entry DOI | 10.2210/pdb4e1v/pdb |
| Descriptor | Uridine phosphorylase, 5-FLUOROURACIL, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | rossmann fold, drug metabolism, transferase |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Cellular location | Cytoplasm (By similarity): P0A1F6 |
| Total number of polymer chains | 9 |
| Total formula weight | 246202.28 |
| Authors | Lashkov, A.A.,Sotnichenko, S.E.,Prokofev, I.I.,Gabdoulkhakov, A.G.,Mikhailov, A.M. (deposition date: 2012-03-07, release date: 2013-03-06, Last modification date: 2023-09-13) |
| Primary citation | Lashkov, A.A.,Sotnichenko, S.E.,Prokofiev, I.I.,Gabdulkhakov, A.G.,Agapov, I.I.,Shtil, A.A.,Betzel, C.,Mironov, A.S.,Mikhailov, A.M. X-ray structure of Salmonella typhimurium uridine phosphorylase complexed with 5-fluorouracil and molecular modelling of the complex of 5-fluorouracil with uridine phosphorylase from Vibrio cholerae. Acta Crystallogr.,Sect.D, 68:968-974, 2012 Cited by PubMed Abstract: Uridine phosphorylase (UPh), which is a key enzyme in the reutilization pathway of pyrimidine nucleoside metabolism, is a validated target for the treatment of infectious diseases and cancer. A detailed analysis of the interactions of UPh with the therapeutic ligand 5-fluorouracil (5-FUra) is important for the rational design of pharmacological inhibitors of these enzymes in prokaryotes and eukaryotes. Expanding on the preliminary analysis of the spatial organization of the active centre of UPh from the pathogenic bacterium Salmonella typhimurium (StUPh) in complex with 5-FUra [Lashkov et al. (2009), Acta Cryst. F65, 601-603], the X-ray structure of the StUPh-5-FUra complex was analysed at atomic resolution and an in silico model of the complex formed by the drug with UPh from Vibrio cholerae (VchUPh) was generated. These results should be considered in the design of selective inhibitors of UPhs from various species. PubMed: 22868762DOI: 10.1107/S090744491201815X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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