Structural Bioinformatics Study of the Structural Basis of Substrate Specificity of Purine Nucleoside Phosphorylase from Thermus thermophilus

Molecular dynamics simulations were performed for wild-type purine nucleoside phosphorylase in complexes with two substrates (adenosine and guanosine). The MD simulations were also performed for the mutant form of the enzyme with the same substrates. The free energy changes upon the formation of the complexes were evaluated from the molecular dynamics trajectories by the MM-GBSA method.

Automated summary

Molecular dynamics simulations were conducted to investigate the complexes of wild-type purine nucleoside phosphorylase with two substrates (adenosine and guanosine), as well as the mutant form of the enzyme with the same substrates. The free energy changes upon complex formation were evaluated using the MM-GBSA method based on the molecular dynamics trajectories.