Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine γ-synthase (XometB) from Xanthomonas oryzae pv. oryzae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1515-7. doi: 10.1107/S1744309112042819. Epub 2012 Nov 14.

Abstract

Cystathionine γ-synthase (CGS) catalyzes the first step in the transsulfuration pathway leading to the formation of cystathionine from O-succinylhomoserine and L-cysteine through a γ-replacement reaction. As an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), CGS from Xoo (XometB) was cloned, expressed, purified and crystallized. The XometB crystal diffracted to 2.4 Å resolution and belonged to the tetragonal space group I4(1), with unit-cell parameters a=b=165.4, c=241.7 Å. There were four protomers in the asymmetric unit, with a corresponding solvent content of 73.9%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Carbon-Oxygen Lyases / chemistry*
  • Carbon-Oxygen Lyases / metabolism
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Xanthomonas / drug effects
  • Xanthomonas / enzymology*
  • Xanthomonas / metabolism

Substances

  • Bacterial Proteins
  • O-succinylhomoserine (thiol)-lyase
  • Carbon-Oxygen Lyases