Determination of 3D structure and properties of cytochrome P450 enzymes in entomopathogenic fungus Beauveria bassiana

To view the motifs in the sequence of the cytochrome P450 amino acids in the pathogenic fungus, Beauveria bassiana, the MOTIF Search site was used and then the motifs were further examined with the Weblogo.v.2.8.2 program. In all sequences, a motif has identified including about 200 amino acids that are related to the P450. This motif was in the sequence 45-96 to about 477-520. The EXXRin helix K and CXG motif with a well-preserved cysteine were identified. While glycine and phenylalanine can be variable. The glycine, dominant amino acid, was at the third position of the motif. In these sequences, asparagine was more dominant. For modeling the proteins, the Mode base program was used. Among the selected models, the model with the lowest e-value and the highest coverage was selected as the best model. Finally, the quality of the designed models was evaluated using the ProSA program with energy calculation and Z-score. In all cases, the energy below zero and the Z-score indicated that the model was appropriate. All models were in the range of 3D structures determined by the X-ray method. Counting the number of alpha helixes and beta pages were carried out with the Stride Web Interface and were 7-18 and 4-13 respectively. The presence of a glycine in the interval between the four amino acids before cysteine and another glycine in the interval between two amino acids afterward led to the formation of two helices in the 3Dprotein structure. It should be noted that the 3D structure of these seven enzymes was first determined in this study.

Keywords:

Amino acids , Motifs , Cytochrome P450 , Entomopathogenic fungus , Modelling