Homology Modeling and Structural Validation Studies of 3 Oxoacyl (Acyl Carrier Protein) Synthase II and Dihydropteroate Synthase Protein of Neisseria meningitides

Vaibhav Sabale and Arun Ingale^*

Department of Biotechnology, School of Life Sciences, North Maharashtra University, Jalgaon, MS, 425001, India

*Corresponding Author : Dr. Arun G. Ingale
Department of Biotechnology, School of Life Sciences, North Maharashtra University, Jalgaon, MS 425001, India
Tel: 0257-2257423
E-mail: agibiotech@gmail.com; agingle@nmu.ac.in

Received: March 23, 2017 Accepted: May 13, 2017 Published: May 19, 2017

Citation: Sabale V, Ingale A (2017) Homology Modeling and Structural Validation Studies of 3 Oxoacyl (Acyl Carrier Protein) Synthase II and Dihydropteroate Synthase Protein of Neisseria meningitides. J Appl Bioinforma Comput Biol 6:2. doi: 10.4172/2329-9533.1000133

Objective: Neisseria meningitidis (NM) is foremost causative agent of bacterial meningitis. The two very important protein has been selected for the study of homology modeling and structural validation in Neisseria meningitis. The 3 oxoacyl (acyl carrier protein) synthase II (3OASII) enzyme which involved in fatty acid biosynthesis of Neisseria meningitidis. This enzyme in fatty acid synthesis and target for discovery of novel antibacterial agent. Dihydropteroate synthase (DHPS), an enzyme plays an acute role in the bacterial folate metabolism which catalyzes the development of 7, 8- dihydropteroate from p-aminobenzoic acid (pABA) and 6- hydroxymethyl-7, 8-dihydropterin-pyrophosphate (DHPP). The absence of the folate pathway in higher eukaryotes makes it an attractive drug target. In current study, a complete 3 oxoacyl (acyl carrier protein) synthase II and Dihydropteroate synthase protein structure model was generated using Modeller V9.12 software so as to understand the mechanistic detail of its functioning. The energy minimization analysis using YASARA and the stereo chemical quality of the models was checked by Rampage, Verfy3D, Errat, ProSA and QMEAN servers. The analysis of present studies provide three dimensional (3D) structure of 3 oxoacyl synthase II and dihydropteroate synthase protein will be helpful for the advance study of drug designing in meningitis disease.
Conclusions: The current study showed that 3 oxoacyl synthase II and Dihydropteroate synthase modeled protein is highly reliable and stable, so it will use to identifying the drug designing research of meningitis disease.