title: Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase.
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.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka 560 012, India.
authors.forename: Vikas
authors.initials: V
authors.lastname: Navratna
authors.forename: Balasubramanian
authors.initials: B
authors.lastname: Gopal
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D006715:Homoserine Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D013211:Staphylococcus aureus / Q000201:enzymology*; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D006715:Homoserine Dehydrogenase
keywords: essential amino-acid metabolism; homoserine dehydrogenase; potential drug target