Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1
Chitinases (EC 3.2.11.14) are capable of hydrolyzing chitins by splitting their ß-1,4-glucosidic bonds. They are present in a wide range of organisms including the fungus Trichoderma virens UKM-1. A gene encoding endochitinase from Trichoderma virens UKM-1 had successfully been cloned (with GenBan...
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my-unisza-ir.21182021-08-15T02:44:09Z http://eprints.unisza.edu.my/2118/ Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 Nadiawati, Alias Nor Muhammad, Mahadi Abdul Munir, Abdul Murad Farah Diba, Abu Bakar S Agriculture (General) Chitinases (EC 3.2.11.14) are capable of hydrolyzing chitins by splitting their ß-1,4-glucosidic bonds. They are present in a wide range of organisms including the fungus Trichoderma virens UKM-1. A gene encoding endochitinase from Trichoderma virens UKM-1 had successfully been cloned (with GenBank Accession number DQ 865246) and expressed in Escherichia coli BL21 (DE3). As a member of glycosyl hydrolases, chitinases are assumed to have a similar catalytic mechanism and structure as other enzymes such as lysozyme. A predicted three dimensional (3D) structure of endochitinase derived from Trichoderma virens UKM-1 was successfully constructed using the Swiss-Prot model server and analyzed by PyMOL software. The prediction of the structure was done by comparing T. virens UKM-1 endochitinase with seven published 3D structures of chitinases from the Swiss-Prot database. Recombinant endochitinase from T. virens UKM-1 was shown to have a TIM-barrel structure with eight parallel ß-sheets and eight α-helices laid down in the inner barrel together with three-stranded ß-sheets. These characteristics revealed the aspects of the catalytic centers of family 18 chitinases. An extensive study was done on the multiple sequence alignment of various class V, family 18 chitinases by using DNASIS Software. Two conserved consensus motif boxes SxGG (Box 1) and DxxDxDxE (Box 2) were found at the N-terminal amino acid sequence of endochitinase from T. virens UKM-1 which were involved in catalysis. 2011 Article NonPeerReviewed text en http://eprints.unisza.edu.my/2118/1/FH02-FPBSM-14-00885.pdf Nadiawati, Alias and Nor Muhammad, Mahadi and Abdul Munir, Abdul Murad and Farah Diba, Abu Bakar (2011) Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1. Title Journal of agrobiotechnology. pp. 83-93. ISSN 1985 5133 |
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S Agriculture (General) Nadiawati, Alias Nor Muhammad, Mahadi Abdul Munir, Abdul Murad Farah Diba, Abu Bakar Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
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Chitinases (EC 3.2.11.14) are capable of hydrolyzing chitins by splitting their ß-1,4-glucosidic bonds.
They are present in a wide range of organisms including the fungus Trichoderma virens UKM-1. A gene
encoding endochitinase from Trichoderma virens UKM-1 had successfully been cloned (with GenBank
Accession number DQ 865246) and expressed in Escherichia coli BL21 (DE3). As a member of
glycosyl hydrolases, chitinases are assumed to have a similar catalytic mechanism and structure as
other enzymes such as lysozyme. A predicted three dimensional (3D) structure of endochitinase
derived from Trichoderma virens UKM-1 was successfully constructed using the Swiss-Prot model
server and analyzed by PyMOL software. The prediction of the structure was done by comparing T.
virens UKM-1 endochitinase with seven published 3D structures of chitinases from the Swiss-Prot
database. Recombinant endochitinase from T. virens UKM-1 was shown to have a TIM-barrel
structure with eight parallel ß-sheets and eight α-helices laid down in the inner barrel together with
three-stranded ß-sheets. These characteristics revealed the aspects of the catalytic centers of family
18 chitinases. An extensive study was done on the multiple sequence alignment of various class V,
family 18 chitinases by using DNASIS Software. Two conserved consensus motif boxes SxGG (Box
1) and DxxDxDxE (Box 2) were found at the N-terminal amino acid sequence of endochitinase
from T. virens UKM-1 which were involved in catalysis. |
format |
Article |
author |
Nadiawati, Alias Nor Muhammad, Mahadi Abdul Munir, Abdul Murad Farah Diba, Abu Bakar |
author_facet |
Nadiawati, Alias Nor Muhammad, Mahadi Abdul Munir, Abdul Murad Farah Diba, Abu Bakar |
author_sort |
Nadiawati, Alias |
title |
Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
title_short |
Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
title_full |
Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
title_fullStr |
Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
title_full_unstemmed |
Three dimensional structure prediction of recombinant endochitinase from trichoderma virens UKM-1 |
title_sort |
three dimensional structure prediction of recombinant endochitinase from trichoderma virens ukm-1 |
publishDate |
2011 |
url |
http://eprints.unisza.edu.my/2118/1/FH02-FPBSM-14-00885.pdf http://eprints.unisza.edu.my/2118/ |
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