title: Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis.
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.
authors: Department of Bioinformatics and Biotechnology, Faculty of Science & Technology, Government College University, Faisalabad, Pakistan.
authors: Ujala
authors: U
authors: Sehar
authors: Muhammad Aamer
authors: MA
authors: Mehmood
authors: Salman
authors: S
authors: Nawaz
authors: Shahid
authors: S
authors: Nadeem
authors: Khadim
authors: K
authors: Hussain
authors: Iqra
authors: I
authors: Sohail
authors: Muhammad Rizwan
authors: MR
authors: Tabassum
authors: Saba Shahid
authors: SS
authors: Gill
authors: Anam
authors: A
authors: Saqib
keywords: B. thuringiensis; CBP24; Molecular docking; homology modeling
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