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Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis

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...

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Autores principales: Sehar, Ujala, Mehmood, Muhammad Aamer, Nawaz, Salman, Nadeem, Shahid, Hussain, Khadim, Sohail, Iqra, Tabassum, Muhammad Rizwan, Gill, Saba Shahid, Saqib, Anam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746096/
https://www.ncbi.nlm.nih.gov/pubmed/23976829
http://dx.doi.org/10.6026/97320630009725
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author Sehar, Ujala
Mehmood, Muhammad Aamer
Nawaz, Salman
Nadeem, Shahid
Hussain, Khadim
Sohail, Iqra
Tabassum, Muhammad Rizwan
Gill, Saba Shahid
Saqib, Anam
author_facet Sehar, Ujala
Mehmood, Muhammad Aamer
Nawaz, Salman
Nadeem, Shahid
Hussain, Khadim
Sohail, Iqra
Tabassum, Muhammad Rizwan
Gill, Saba Shahid
Saqib, Anam
author_sort Sehar, Ujala
collection PubMed
description 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.
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spelling pubmed-37460962013-08-23 Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis Sehar, Ujala Mehmood, Muhammad Aamer Nawaz, Salman Nadeem, Shahid Hussain, Khadim Sohail, Iqra Tabassum, Muhammad Rizwan Gill, Saba Shahid Saqib, Anam Bioinformation Hypothesis 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. Biomedical Informatics 2013-08-07 /pmc/articles/PMC3746096/ /pubmed/23976829 http://dx.doi.org/10.6026/97320630009725 Text en © 2013 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Sehar, Ujala
Mehmood, Muhammad Aamer
Nawaz, Salman
Nadeem, Shahid
Hussain, Khadim
Sohail, Iqra
Tabassum, Muhammad Rizwan
Gill, Saba Shahid
Saqib, Anam
Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title_full Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title_fullStr Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title_full_unstemmed Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title_short Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
title_sort three dimensional (3d) structure prediction and substrate-protein interaction study of the chitin binding protein cbp24 from b. thuringiensis
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746096/
https://www.ncbi.nlm.nih.gov/pubmed/23976829
http://dx.doi.org/10.6026/97320630009725
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