Abstract
Bacillus thuringiensis
is an insecticidal bacterium whose chitinolytic system has been exploited to improve insect resistance in crops.
In the present study, we studied the CBP24 from
B. thuringiensis
using homology modeling and molecular docking. The primary
and secondary structure analyses showed CBP24 is a positively charged protein and contains single domain that belongs to family
CBM33. The 3D model after refinement was used to explore the chitin binding characteristics of CBP24 using AUTODOCK. The
docking analyses have shown that the surface exposed hydrophilic amino acid residues Thr-103, Lys-112 and Ser-162 interact with
substrate through H-bonding. While, the amino acids resides Glu-39, Tyr-46, Ser-104 and Asn-109 were shown to have polar
interactions with the substrate. The binding energy values evaluation of docking depicts a stable intermolecular conformation of
the docked complex. The functional characterization of the CBP24 will elucidate the substrate-interaction pathway of the protein in
specific and the carbohydrate binding proteins in general leading towards the exploration and exploitation of the prokaryotic
substrate utilization pathways.