Homology modeling, molecular docking and electrostatic potential analysis of MurF ligase from Klebsiella pneumonia.

ABSTRACT: In spite of availability of moderately protective vaccine and antibiotics, new antibacterial agents are urgently needed to decrease the global incidence of Klebsiella pneumonia infections. MurF ligase, a key enzyme, which participates in the bacterial cell wall assembly, is indispensable to existence of K. pneumonia. MurF ligase lack mammalian vis-à-vis and have high specificity, uniqueness, and occurrence only in eubacteria, epitomizing them as promising therapeutic targets for intervention. In this study, we present a unified approach involving homology modeling and molecular docking studies on MurF ligase enzyme. As part of this study, a homology model of K. pneumonia (MurF ligase) enzyme was predicted for the first time in order to carry out structurebased drug design. The accuracy of

SUBMITTER: Sivaramakrishnan V 

PROVIDER: S-EPMC3374357 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature