Insights from the Molecular Dynamics Simulation of Cellobiohydrolase Cel6A Molecular Structural Model from Aspergillus fumigatus NITDGPKA3.
2016
Global demand for bioethanol is increasing tremendously as it could help to replace the
conventional fossil fuel and at the same time supporting the bioremediation of huge volume of
cellulosic wastes generated from different sources. Ideal genetic engineering approaches are essential
to improve the efficacy of the bioethanol production processes for real time applications. A locally
isolated fungal strain Aspergillus fumigatus NITDGPKA3 was used in our laboratory for the
hydrolysis of lignocellulose with good cellulolytic activity when compared with other contemporary
fungal strains. An attempt is made to sequence the cellobiohydrolases (CBHs) of A. fumigatus
NITDGPKA3, model its structure to predict its catalytic activity towards improving the protein by genetic engineering
approaches. Herein, the structure of the sequenced Cellobiohydrolases (CBHs) of A. fumigatus NITDGPKA3, modelled
by homology modelling and its validation is reported. Further the catalytic activity of the modelled CBH enzyme was
assessed by molecular docking analysis. Phylogenetic analysis showed that CBH from A. fumigatus NITDGPKA3 belongs
to the Glycohydro 6 (Cel6A) super family. Molecular modeling and molecular dynamics simulation suggest the structural
and functional mechanism of the enzyme. The structures of both the cellulose binding (CBD) and catalytic domain (CD)
have been compared with most widely studied CBH of Trichoderma reesei. The molecular docking with cellulose
suggests that Gln 248, Pro 287, Val236, Asn284, and Ala288 are the main amino acids involved in the hydrolysis of the β,
1-4, glycosidic bonds of cellulose.
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