©1996-2019. All
Rights Reserved. Online Journal of Bioinformatics . You may not store
these pages in any form except for your own personal use. All other usage or
distribute on is illegal under international copyright treaties. Permission to
use any of these pages in any other way besides the before mentioned
must be gained in writing from the publisher. This article is exclusively
copyrighted in its entirety to OJB publications. This article may be copied
once but may not be, reproduced or
re-transmitted without the express permission of the
editors. This journal satisfies the refereeing requirements (DEST)
for the Higher Education Research Data Collection (Australia). Linking:To link to this page or
any pages linking to this page you must link directly to this page only here
rather than put up your own page.
OJBTM
Online Journal of Bioinformatics ©
Volume 12(2):217-229, 2011
Homology modeling and active
site analysis of MurB Reductase: A potential drug target
of Legionella pneumophila
Vani Priyadarshini (MSc), Dibyabhaba Pradhan (MSc), Manne Munikumar
(MSc) and Amineni Umamaheswari
(PhD)*
SVIMS Bioinformatics Centre,
Department of Bioinformatics, SVIMS University, Tirupati,
PIN: 517507, India. Email: svims.btisnet@nic.in
ABSTRACT
Priyadarshini V, Pradhan D,
Munikumar M, Umamaheswari
A., Homology Modeling and Active Site Analysis of MurB
Reductase: A Potential Drug Target of Legionella pneumophila,
Onl J Bioinform., 12(2):217-229,
2011. Legionella pneumophila is increasingly recognized as a significant cause of
Legionnaires’ disease, pneumonia and life-threatening prosthetic valve
endocarditis in ambulatory and hospitalized patients. The severe consequences
of these disease demands the need to gain insight on novel drug targets of L. pneumophila for
facilitating rational drug design.
UDP-N- acetyl enolpyruvoyl glucosamine
reductase (MurB) plays a vital role in peptidoglycan
biosynthesis by catalyzing UDP-N-acetylglucosamine enolpyruvate to UDP-N-acetylmuramic
acid. There is no alternative mechanism in L.
pneumophila to substitute catalytic activity
rendered by MurB and was selected as a potential
molecular target against the pathogen. Homology modeling method was
accomplished to construct MurB tertiary structure
incorporating FAD using Modeller9v8. The predicted structure was validated
through DOPE score correlation, superpose, PROCHECK and ProSA.
The predicted structure being highly reliable was submitted to the protein
model database (PMDB) that accepted the structure with less than 3% stereo
chemical check failure. Ligand binding site residues were located from MurB model in complex with FAD using PyMOL,
LIGPLOT and CASTp. Structural, functional and active
site information on MurB of L. pneumophila would aid in rational drug
design for novel drug discovery to combat the pathogen.
Keywords:
Legionnaires’ disease, Bronchopneumonia, MurB,
Homology modeling
FULL-TEXT(SUBSCRIPTION OR PURCHASE TITLE $25USD)