Paper
Structural Characterization and Active Site Prediction of Bacterial Keratinase through Molecular Docking
- Authors:
- Amrita Banerjee; Dipak K. Sahoo; Hrudayanath Thatoi; Bikash R. Pati; Keshab C. Mondal; Arnab Sen; Pradeep K. Das Mohapatra
- Abstract
- Keratinase (EC 3.4.99), a proteolytic enzyme has been classified by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) as a group of proteinases with an unknown mechanism. The present study is an initiative for deeper insight towards mechanism of action. The in silico analysis of fifteen bacterial keratinase sequences showed the elucidation of consensus regions, superfamily/family classification, phylogenetic tree and; conserved motifs. Six different species specific energy minimized protein structures were found using threading. Quality assessment of these structures represented a common structure from ten Bacillus species with a high quality value. This structure had been selected for hydrophobicity and solvent accessibility to surface. The sequence of selected structure of Bacillus genus showed 100% sequence similarity with alkaline serine protease of Bacillus licheniformis (Acc. No. AAZ77709.1), which proved to be a serine protease. Finally, molecular docking studies were performed with phenylmethylsulfonyl fluoride (PMSF) to predict the enzymes active site, as PMSF irreversibly binds to the active site serine residue of serine protease. A total of ten docking sites were found among them. Two of them were selected and predicted as the active sites of keratinase belonging to Bacillus genus.
- Keywords
- Multiple Sequence Alignment; Superfamily; Phylogenetic Tree; Motif; 3D-Structure; Ramachandran Plot; Energy Minimization; Molecular Docking
- StartPage
- 67
- EndPage
- 82
- Doi