Abstract: Identification of novel drug targets in silico in Vibrio
vulnificus is important as it is one of the emerging pathogenic
microorganisms. Glutamate racemase, an important constituent of bacterial cell
wall is chosen for structure prediction using homology modeling. With the aid
of tools and softwares like MODELLER and Swiss-PdbViewer, the 3D structure is
predicted and the final model is refined by energy minimization. The quality of
the refined model is assessed using PROCHECK. The interaction between the
predicted structure of glutamate racemase and its potential inhibitors namely
L-serine O-sulfate,
(2R,4R)-2-amino-4-(2-benzo[b]thienyl)methyl
pentanedioic acid, aziridino glutamate, exiguaquinol, γ-2
naphthylmethyl-D-glutamate and D-glutamine is analysed in
silico by Autodock. The results indicate that certain residues like Asp13,
Tyr45, Gly46, Asn78, Thr79, Cys185, His187 are highly conserved across the
active site stretches of different bacterial species and may possibly assume
precedence over the other residues for inhibitory action. This study provides
an insight into the structure of glutamate racemase in V. vulnificus and
also gives an idea about potential sites responsible for inhibitory action that
could further be substantiated by experimental investigations.
