Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 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...

Full description

Bibliographic Details
Main Authors:	Noorbatcha, Ibrahim Ali, Sultan, Anas Mufid Nasri, Amid, Azura, Mohd. Salleh, Hamzah
Format:	Article
Language:	English
Published:	Research Journal of Chemistry and Environment 2010
Subjects:	QD Chemistry
Online Access:	http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf

id	iium-2365
recordtype	eprints
spelling	iium-23652011-11-16T02:58:33Z http://irep.iium.edu.my/2365/ Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah QD Chemistry 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 ASUIA243 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 ASUIA243 model with 71.268% sequence identity. Both models were evaluated and found to be quite satisfactory without being manually modified. These models can now be used in protein structural studies to improve properties such as specific activity, pH tolerance and thermostability. Research Journal of Chemistry and Environment 2010-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf Noorbatcha, Ibrahim Ali and Sultan, Anas Mufid Nasri and Amid, Azura and Mohd. Salleh, Hamzah (2010) Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases. Research Journal of Chemistry and Environment, Specil (issue). pp. 318-323. ISSN 0972-0626 http://www.chemenviron.net/RJCE/RJCE/right.htm
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QD Chemistry
spellingShingle	QD Chemistry Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 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 ASUIA243 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 ASUIA243 model with 71.268% sequence identity. Both models were evaluated and found to be quite satisfactory without being manually modified. These models can now be used in protein structural studies to improve properties such as specific activity, pH tolerance and thermostability.
format	Article
author	Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah
author_facet	Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah
author_sort	Noorbatcha, Ibrahim Ali
title	Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
title_short	Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
title_full	Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
title_fullStr	Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
title_full_unstemmed	Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
title_sort	homology modelling and structural analysis of phyfauia1_h and bacillus subtilis asuia243 phytases
publisher	Research Journal of Chemistry and Environment
publishDate	2010
url	http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf
first_indexed	2023-09-18T20:09:57Z
last_indexed	2023-09-18T20:09:57Z
_version_	1777407411351453696

Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases

Similar Items