In silico analysis and 3D structure prediction of a chitinase from psychrophilic yeast Glaciozyma antarctica PI12
Chitinases are a group of glycosyl hydrolases that are essential to recycle chitin presence in nature. The aim of this work is to characterise the sequence of a chitinase isolated from a psychrophilic yeast, Glaciozyma antarctica PI12 and to predict and analyse the 3-dimensional protein structure....
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Penerbit Universiti Kebangsaan Malaysia
2017
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| Online Access: | http://journalarticle.ukm.my/12310/ http://journalarticle.ukm.my/12310/ http://journalarticle.ukm.my/12310/1/46_01_17.pdf |
| Summary: | Chitinases are a group of glycosyl hydrolases that are essential to recycle chitin presence in nature. The aim of this work is to
characterise the sequence of a chitinase isolated from a psychrophilic yeast, Glaciozyma antarctica PI12 and to predict and
analyse the 3-dimensional protein structure. The cDNA for the G. antarctica chitinase gene, GaCHT43, with a length of
1,176 bp was reverse transcribed from mRNA, cloned and sequenced. The gene encodes a mature protein of 391 amino
acids with an expected molecular weight of 43 kDa. Sequence analysis showed that GaCh43 has high similarity to the
endochitinase family 18 proteins of other fungi. A three-dimensional (3D) model of GaCht43 was built by homology modelling
with Aspergillus fumigatus chitinase (1W9P) as the template. Validation analysis via PROCHECK, VERIFY3D and ERRAT
showed that the GaCht43 model surpassed the quality requirements and was accepted for further analysis. GaCht43 contained
chitinase conserved regions, SxGG and DxxDxDxE that are required in the catalytic mechanism. Analysis of the GaCht43
structure showed the presence of extra loop regions compared to mesophilic chitinases, which might contribute to the flexibility
of the protein. |
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