Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1216-9. doi: 10.1107/S1744309113025803. Epub 2013 Oct 17.

Abstract

Staphylococcus aureus is a Gram-positive nosocomial pathogen. The prevalence of multidrug-resistant S. aureus strains in both hospital and community settings makes it imperative to characterize new drug targets to combat S. aureus infections. In this context, enzymes involved in cell-wall maintenance and essential amino-acid biosynthesis are significant drug targets. Homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine.

Keywords: essential amino-acid metabolism; homoserine dehydrogenase; potential drug target.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Homoserine Dehydrogenase / chemistry*
  • Homoserine Dehydrogenase / isolation & purification
  • Hydrogen-Ion Concentration
  • Staphylococcus aureus / enzymology*
  • Temperature
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Homoserine Dehydrogenase