Structural binding analysis of native and mutant Nomascus Acetyl CoA binding proteins using in silico methods

Abstract

Acyl-CoA binding protein (ACBP) having molecular weight of 10kDa is known to bind to C12-C22 acyl-CoA esters. The ACBP proteins are highly conserved across phylum as their homologues have been identified in all four eukaryotic kingdoms and 11 species of eubacteria most of which are pathogenic. The 3-D structures of some ACBPs were determined using X-ray crystallography and NMR spectroscopy, which showed four -helices fixed in a skew shape with acyl-CoAbinding site. Using in silico method Clustal W, we identified five residues. These residues are point mutated modeled by using Discovery Studio software to analyze static structural properties as well as dynamic behavior with respect to wild type, using GROMACS software for molecular dynamic simulations. In present study, we modeled acbp mutants (ala36-> gly) computationally and analyzed structure properties with molecular dynamics tools and analyzed parameters like RMSD, RMSF, radius of gyration, H-bond. We performed docking studies with myristyl and palmityl CoA with different docking tools and observed significant binding energy in both ligands indicating that mutation doesn’t affect any property of modeled ACBP protein.