Expression, purification, crystallization and preliminary X-ray analysis of ribitol-5-phosphate cytidylyltransferase from Bacillus subtilis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1195-7. doi: 10.1107/S1744309112035142. Epub 2012 Sep 26.

Abstract

TarI is a ribitol-5-phosphate cytidylyltransferase that catalyzes the formation of CDP-ribitol, which is involved in the biosynthesis of wall teichoic acids, from CTP and ribitol 5-phosphate. TarI from Bacillus subtilis (BsTarI) was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.78 Å and belonged to the monoclinic space group C2, with unit-cell parameters a = 103.74, b = 60.97, c = 91.80 Å, β = 113.48°. The initial structural model indicated that the crystals of BsTarI contained a dimer in the asymmetric unit.

MeSH terms

  • Bacillus subtilis / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Models, Molecular
  • Nucleotidyltransferases / chemistry*
  • Nucleotidyltransferases / genetics
  • Nucleotidyltransferases / isolation & purification
  • Protein Structure, Tertiary

Substances

  • Nucleotidyltransferases
  • D-ribitol-5-phosphate cytidylyltransferase