WASET
	%0 Journal Article
	%A Jayashree Ramana
	%D 2013
	%J International Journal of Medical and Health Sciences
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 79, 2013
	%T Novel Structural Insights of Glutamate Racemase from Mycobacterium tuberculosis through Modeling and Docking Studies
	%U https://publications.waset.org/pdf/16514
	%V 79
	%X An alarming emergence of multidrug-resistant strains
of the tuberculosis pathogen Mycobacterium tuberculosis and
continuing high worldwide incidence of tuberculosis has invigorated
the search for novel drug targets. The enzyme glutamate racemase
(MurI) in bacteria catalyzes the stereoconversion of L-glutamate to
D-glutamate which is a component of the peptidoglycan cell wall of
the bacterium. The inhibitors targeted against MurI from several
bacterial species have been patented and are advocated as promising
antibacterial agents. However there are none available against MurI
from Mycobacterium tuberculosis, due to the lack of its threedimensional
structure. This work accomplished two major objectives.
First, the tertiary structure of MtMurI was deduced computationally
through homology modeling using the templates from bacterial
homologues. It is speculated that like in other Gram-positive bacteria,
MtMurI exists as a dimer and many of the protein interactions at the
dimer interface are also conserved. Second, potent candidate
inhibitors against MtMurI were identified through docking against
already known inhibitors in other organisms.

	%P 418 - 422