Comparison stability Rusticyanin 23270 wild-type and mutant His143Leu using molecular dynamics simulation

Abstract

The Acidithiobacillus ferroxidans bacterium plays an important role in the bioleaching process of uranium. The rusticyanin protein is the second most crucial component in the electron transport chain in the membrane of the Acidithiobacillus ferroxidnas bacterium. This protein belongs to the large family of copper blue proteins. The protein sequence rusticyanin 23270 was derived from UniProtKB database. A suitable template for modeling was prepared from the Swiss model server, and the best protein model was made with Modeller software. The His143Leu mutation was developed using the Pymol software in the protein. The effect of the mutation on the stability of the protein structure was investigated by analysing the results of molecular dynamics simulation on the wild-type and mutant protein. The values RMSD and RMSF are the same for both wild-type and mutant. The amount of Rg in mutant protein is reduced. His143Leu mutation in the rusticyanin 23270 protein does not affect the secondary structure protein and slightly increases the folding and stability of the tertiary structure.