Structure prediction of a putative restriction endonuclease (AbaSORF13P) from Acinetobacter baumannii SDF

Restriction enzymes represent a class of endonucleases that cleave DNA in a specific manner. They are widely used in recombinant DNA technology and known as molecular scissors. In this communication, a putative restriction endonucleases from (Acinetobacter baumannii SDF) was identified in NCBI database, and characterized for biophysical properties, sequence homology and a structural modeling. This putative restriction enzyme (AbaSORF13P) shows Molecular Mass equal to 41kDa with high content of aromatics amino acids. In homology search, the enzyme was found to be a member of PLD superfamily. It showed very high sequence similarity with known restriction enzymes BmrI and BfiI. The tertiary structure of the enzyme was determined on the basis homology modeling at SWISS-MODEL workspace using BfiI as the template. The enzyme was found to the made up of two subunits joined together in an asymmetric manner. These studies confirm, restriction endonuclease like behavior of the hypothetical protein, and these findings will be very important in characterization of the enzyme in vitro.