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 GenB...
Saved in:
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
2011
|
Subjects: | |
Online Access: | http://eprints.unisza.edu.my/3078/1/FH02-FPBSM-14-00885.pdf http://eprints.unisza.edu.my/3078/ |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | 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. |
---|