Crystal structure of Escherichia coli xanthine phosphoribosyltransferase.

@article{Vos1997CrystalSO,
  title={Crystal structure of Escherichia coli xanthine phosphoribosyltransferase.},
  author={Siska Vos and John de Jersey and Jennifer L. Martin},
  journal={Biochemistry},
  year={1997},
  volume={36 14},
  pages={4125-34}
}
Xanthine phosphoribosyltransferase (XPRT; EC 2.4.2.22) from Escherichia coli is a tetrameric enzyme having 152 residues per subunit. XPRT catalyzes the transfer of the phosphoribosyl group from 5-phospho-alpha-D-ribosyl 1-pyrophosphate (PRib-PP) to the 6-oxopurine bases guanine, xanthine, and hypoxanthine to form GMP, XMP, and IMP, respectively. Crystals grown in the absence of substrate or product were used to determine the structure of XPRT at a resolution of 1.8 A, by multiple isomorphous… CONTINUE READING