Title : DMSO enhanced conformational switch of an interfacial enzyme - Lindsay_2016_Biopolymers_105_864 |
Author(s) : Lindsay RJ , Johnson QR , Evangelista W , Nellas RB , Shen T |
Ref : Biopolymers , 105 :864 , 2016 |
Abstract :
Interfacial proteins function in unique heterogeneous solvent environments, such as water-oil interfaces. One important example is microbial lipase, which is activated in an oil-water emulsion phase and has many important enzymatic functions. A unique aprotic dipolar organic solvent, dimethyl sulfoxide (DMSO), has been shown to increase the activity of lipases, but the mechanism behind this enhancement is still unknown. Here, all-atom molecular dynamics simulations of lipase in a binary solution were performed to examine the effects of DMSO on the dynamics of the gating mechanism. The amphiphilic alpha5 region of the lipase was a focal point for the analysis, since the structural ordering of alpha5 has been shown to be important for gating under other perturbations. Compared to the closed-gorge ensemble in an aqueous environment, the conformational ensemble shifts towards open-gorge structures in the presence of DMSO solvents. Increased width of the access channel is particularly prevalent in 45% and 60% DMSO concentrations (w/w). As the amount of DMSO increases, the alpha5 region of the lipase becomes more alpha-helical, as we previously observed in studies that address water-oil interfacial and high pressure activation. We believe that the structural ordering of alpha5 plays an essential role on gating and lipase activity. |
PubMedSearch : Lindsay_2016_Biopolymers_105_864 |
PubMedID: 27463323 |
Lindsay RJ, Johnson QR, Evangelista W, Nellas RB, Shen T (2016)
DMSO enhanced conformational switch of an interfacial enzyme
Biopolymers
105 :864
Lindsay RJ, Johnson QR, Evangelista W, Nellas RB, Shen T (2016)
Biopolymers
105 :864