Chitin deacetylases are enzymes responsible for structuring chitin of chitin-producing organisms. Chitin deacetylases are well studied in fungi and bacteria, but the canonical structure was just recently characterized for an insect, the silk moth Bombyx mori (Lepidoptera: Bombycidae) (PDB: 5ZNT; 5ZNS). The whitefly Bemisia tabaci (Hemiptera: Aleyrodidae) is a polyphagous insect that causes severe loses in agriculture every year and there is a lack of new and safer modes of action for controlling such pest. In the present study, the three-dimensional structure of B. tabaci chitin deacetylase was modeled discussed using as model the newly insect chitin deacetylase described. Firstly, by BLAST, the amino acid sequence of B. tabaci chitin deacetylase was obtained from GenBank according to its identity to B. mori chitin deacetylase. The three-dimensional model and quality estimation of B. tabaci chitin deacetylase was obtained by Swiss-Model tool. Active sites, chitin binding site and the overall structure of B. tabaci chitin deacetylase were observed to be in agreement to the crystal structure of B. mori chitin deacetylase. It is expected that three-dimensional model of chitin deacetylases may be valuable for rational pesticide design. Further, other molecular targets can be searched and studied with the same in silico tools.
Keywords: Bombyx mori, whitefly, insect, polyphagous, three-dimensional.