Modeling and determining the structures and characteristics of cytochrome P450 enzymes in the entomopathogenic fungus, Beauveria bassiana

Cytochrome P450 enzymes are a large family of proteins containing haem and play an important role in metabolism of various compounds. Entomopathogenic fungus, Beauveria bassiana also contains these enzymes for targeting insect alkanes. The aim of this study was to investigate the properties and protein structure of seven cytochrome P 450 enzymes in this fungus and to predict the three-dimensional structure of these enzymes by homology modeling method.

Predicting possible situations with intracellular helices was performed with the TMHMM program. SignalP4.1 program was used to predict the probability of the presence and location of shear sites of signal peptides in amino acid sequences. Some of the physical and chemical parameters of the proteins were performed with the ProtParam program. The modeling was conducted in the Modebase database.

In all sequences, a motif was identified and had about 200 amino acids that were related to P450. The motif was in the sequence of 96-45 to about 477-520. CYP539B5 and CYP52G11 proteins were stable. CYP584Q1 had the highest and CYP617N1 had the lowest hydrophilic acid of all. Among the selected models, the model with lowest e-value and the highest coverage was selected as the best model. CYP5337A1 and CYP52G11 lacked helix and CYP617N1 had two helices. Number of estimated amino acids in the helices, in all cases except CYP584Q1, CYP5337A1 and CYP52G11, was greater than 18. No signal peptide was detected.

In this study, the modeled structures of seven cytochrome P450 enzymes were reported for the first time in the fungus B. bassiana. The enzymes' stability and their resistance to adverse environmental factors such as temperature and UV can increase the fungal pathogenicity against the pests.