Homology modelling and structural analysis of Phytases

Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable techniq...

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Main Authors:	Noorbatcha, Ibrahim Ali, Mohd. Salleh, Hamzah, Amid, Azura
Format:	Conference or Workshop Item
Language:	English
Published:	2010
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/4071/ http://irep.iium.edu.my/4071/ http://irep.iium.edu.my/4071/4/IRIIE2010_Homology__Poster.pdf

id	iium-4071
recordtype	eprints
spelling	iium-40712011-11-21T19:49:57Z http://irep.iium.edu.my/4071/ Homology modelling and structural analysis of Phytases Noorbatcha, Ibrahim Ali Mohd. Salleh, Hamzah Amid, Azura TP248.13 Biotechnology Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable technique in solving proteins’ 3D structures, starting from their amino acid sequences. In this study, homology modelling was used to obtain the 3D structure of two different phytases using only their amino acid sequence; phyFAUIA1_H which belongs to the histidine acid phosphatases, and Bacillus subtilis SAUIA243 which belongs to the β-propeller phytases. E. coli phytase (PDB code 1dkm) was used as a template for phyFAUIA1_H model with 99.512% sequence identity. On the other hand, Bacillus amyloliquefaciens (PDB code 2poo) was used as a template for B. subtilis SAUIA243 model with 71.268% sequence identity. The BLAST (Basic Local Alignment Search Tool) algorithm was used to find the highest scoring ungapped local alignment between the query and database sequences. This particular score uses the BLOSUM substitution matrix, which is a block substitution matrix that uses segments of blocks corresponding to the most highly conserved regions of proteins. Both models were evaluated and found to be quite satisfactory without being manually modified. Phytases are important constituents in Animal feed industry. These models can now be used to design new phytases, with improve properties such as enhanced enzyme activity, pH tolerance, and thermostability. 2010-01-26 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/4071/4/IRIIE2010_Homology__Poster.pdf Noorbatcha, Ibrahim Ali and Mohd. Salleh, Hamzah and Amid, Azura (2010) Homology modelling and structural analysis of Phytases. In: IIUM Research, Innovation & Invention Exhibition (IRIIE 2010), 26 - 27 January 2010, Kuala Lumpur. (Unpublished) http://www.iium.edu.my/irie/10/sub10/author/list_p.php
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Noorbatcha, Ibrahim Ali Mohd. Salleh, Hamzah Amid, Azura Homology modelling and structural analysis of Phytases
description	Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable technique in solving proteins’ 3D structures, starting from their amino acid sequences. In this study, homology modelling was used to obtain the 3D structure of two different phytases using only their amino acid sequence; phyFAUIA1_H which belongs to the histidine acid phosphatases, and Bacillus subtilis SAUIA243 which belongs to the β-propeller phytases. E. coli phytase (PDB code 1dkm) was used as a template for phyFAUIA1_H model with 99.512% sequence identity. On the other hand, Bacillus amyloliquefaciens (PDB code 2poo) was used as a template for B. subtilis SAUIA243 model with 71.268% sequence identity. The BLAST (Basic Local Alignment Search Tool) algorithm was used to find the highest scoring ungapped local alignment between the query and database sequences. This particular score uses the BLOSUM substitution matrix, which is a block substitution matrix that uses segments of blocks corresponding to the most highly conserved regions of proteins. Both models were evaluated and found to be quite satisfactory without being manually modified. Phytases are important constituents in Animal feed industry. These models can now be used to design new phytases, with improve properties such as enhanced enzyme activity, pH tolerance, and thermostability.
format	Conference or Workshop Item
author	Noorbatcha, Ibrahim Ali Mohd. Salleh, Hamzah Amid, Azura
author_facet	Noorbatcha, Ibrahim Ali Mohd. Salleh, Hamzah Amid, Azura
author_sort	Noorbatcha, Ibrahim Ali
title	Homology modelling and structural analysis of Phytases
title_short	Homology modelling and structural analysis of Phytases
title_full	Homology modelling and structural analysis of Phytases
title_fullStr	Homology modelling and structural analysis of Phytases
title_full_unstemmed	Homology modelling and structural analysis of Phytases
title_sort	homology modelling and structural analysis of phytases
publishDate	2010
url	http://irep.iium.edu.my/4071/ http://irep.iium.edu.my/4071/ http://irep.iium.edu.my/4071/4/IRIIE2010_Homology__Poster.pdf
first_indexed	2023-09-18T20:12:09Z
last_indexed	2023-09-18T20:12:09Z
_version_	1777407549004316672

Homology modelling and structural analysis of Phytases

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