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

Navratna, Vikas and Gopal, Balasubramanian (2013) Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase. In: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 69 (11). pp. 1216-1219.

PDF Act_Cry_sec_str_Bio_cry_com_69_1216_2013.pdf - Published Version Restricted to Registered users only Download (366kB) | Request a copy

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.

Item Type:	Journal Article
Publication:	ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Publisher:	WILEY-BLACKWELL
Additional Information:	copyright for this article belongs to WILEY-BLACKWELL,USA
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	23 Dec 2013 05:25
Last Modified:	23 Dec 2013 05:25
URI:	http://eprints.iisc.ac.in/id/eprint/47963

Actions (login required)

View Item