The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution

Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):51-60. doi: 10.1107/S0907444909044175. Epub 2009 Dec 21.

Abstract

Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 A resolution (R(cryst) = 17.6%, R(free) = 20.6%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Ions / chemistry
  • Macromolecular Substances / chemistry*
  • Phosphates / chemistry
  • Potassium / chemistry
  • Protein Conformation
  • Salmonella typhimurium / enzymology*
  • Uridine / analogs & derivatives
  • Uridine / chemistry*
  • Uridine / pharmacology
  • Uridine Phosphorylase / chemistry*
  • Uridine Phosphorylase / metabolism

Substances

  • Bacterial Proteins
  • Ions
  • Macromolecular Substances
  • Phosphates
  • Uridine Phosphorylase
  • Potassium
  • Uridine

Associated data

  • PDB/3FWP