4E1V

X-RAY Structure of the Uridine Phosphorylase from Salmonella Typhimurium in Complex with 5-Fluorouracil at 2.15 A Resolution

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4E1V の概要

• エントリーDOI: 10.2210/pdb4e1v/pdb
• 分子名称: Uridine phosphorylase, 5-FLUOROURACIL, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: rossmann fold, drug metabolism, transferase
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• 細胞内の位置: Cytoplasm (By similarity): P0A1F6
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 246202.28

構造登録者

Lashkov, A.A.,Sotnichenko, S.E.,Prokofev, I.I.,Gabdoulkhakov, A.G.,Mikhailov, A.M. (登録日: 2012-03-07, 公開日: 2013-03-06, 最終更新日: 2023-09-13)

主引用文献

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

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: 22868762
DOI: 10.1107/S090744491201815X

実験手法

X-RAY DIFFRACTION (2.15 Å)