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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2013
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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. |
format | Online Article Text |
id | pubmed-3746096 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
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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