Hydrophobic interactions induced activation of a thermo-alkalophilic lipase from Geobacillus SBS-4S by molecular dynamics simulations

Recently,we have reported the 3-dimensional structure of the lipase (lipsbs) from geobacillus sbs-4s in closed configuration by x-ray crystallography. in the present study,we report on activation of the close configuration of lipsbs to its open form. the presence of metal ions or a non-ionic detergent in the crystallization buffer could not activate lipsbs. however,addition of octane molecules initiated upward movement of the lid,leaving rest of the protein intact,by molecular dynamics simulations. the hydrophobic interactions between amino acids of the lid and octane molecules resulted in shifting the inactive configuration to the active one. these results were reinforced by root-mean-sqaure deviation (rmsd) data. our data shed light on the structural changes that take place during activation of lipsbs.