Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori

Mol Cells. 2003 Jun 30;15(3):361-3.

Abstract

Orotic acid phosphoribosyltransferase (PyrE) (EC 2.4.2.10) is a key enzyme in de novo uridine monophosphate (UMP) biosynthesis. It catalyzes the reaction between orotic acid and 5-phosphoribosyl-1-pyrophosphate (PRPP) to yield orotidine monophosphate (OMP), which is transformed to uridine monophosphate by decarboxylation. H. pylori PyrE was crystallized at 294 +/- 1 K by the hanging drop vapor-diffusion method. The crystals belong to the space group P2(1)2(1)2(1) with unit-cell dimensions a = 95.8, b = 104.9, c = 281.1 A, alpha = beta = gamma = 90 degrees. A set of diffraction data was collected to 3.29 A resolution using synchrotron X-ray radiation.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods*
  • Crystallography, X-Ray / methods*
  • Escherichia coli / genetics
  • Helicobacter pylori / enzymology*
  • Orotate Phosphoribosyltransferase / chemistry*
  • Protein Conformation
  • Salmonella typhimurium / genetics
  • Sequence Alignment
  • Transfection

Substances

  • Orotate Phosphoribosyltransferase