Homology modeling and site-directed mutagenesis of chitinase fromStreptomyces griseolosporeus

Chitin is the second most abundant biopolymer on the earth after cellulose. Chitinases are glycosyl hydrolases that catalyze the conversion of chitin biopolymer to low molecular weight chitooligomers, have a wide variety of biotechnological and industrial applications. Template crystal structure of chitinase from Streptomycesgriseus (PDB ID: 1wvu) was used for homology modeling of the enzyme (UniProt ID:A0A0D0Q8E2) using Modeler software. The model was loop refined and was validated using RMSD, ProSA, and PROCHECK. The refined model was submitted to the Protein Model Data Base. The docking was carried out to elucidate the interaction energies of amino acid residues with the chitin ligand, obtained from the ChemSpider database. To enhance the binding of chitin with the enzyme, mutation studies were carried out by replacing Thr14 as it had a less interaction energy. Out of 10 mutants were selected using the PoPMuSiC server. The favorable mutant for binding of chitin was chosen based on RMSD and RMSF of MD simulations. Thus, modeling chitinase would aid in the detailed understanding of its structural properties and mutation studies would help in improving the enzyme efficiency

کلیدواژه ها:

Chitinase ، Homology modeling ، Docking ، Mutation and molecular dynamics