Shaposhnikova_2021_Crystals_11_1052

Reference

Title : Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids - Shaposhnikova_2021_Crystals_11_1052
Author(s) : Shaposhnikova A , Kuty M , Chaloupkova R , Damborsky J , Smatanova IK , Minofar B , Prudnikova T
Ref : Crystals , 11 :1052 , 2021
Abstract :

Ionic liquids attracted interest as green alternatives to replace conventional organic solvents in protein stability studies. They can play an important role in the stabilization of enzymes such as haloalkane dehalogenases that are used for biodegradation of warfare agents and halogenated environmental pollutants. Three-dimensional crystals of haloalkane dehalogenase variant DhaA80 (T148L+G171Q+A172V+C176F) from Rhodococcus rhodochrous NCIMB 13064 were grown and soaked with the solutions of 2-hydroxyethylammonium acetate and 1-butyl-3-methylimidazolium methyl sulfate. The objective was to study the structural basis of the interactions between the ionic liquids and the protein. The diffraction data were collected for the 1.25 A resolution for 2-hydroxyethylammonium acetate and 1.75 A resolution for 1-butyl-3-methylimidazolium methyl sulfate. The structures were used for molecular dynamics simulations to study the interactions of DhaA80 with the ionic liquids. The findings provide coherent evidence that ionic liquids strengthen both the secondary and tertiary protein structure due to extensive hydrogen bond interactions.

PubMedSearch : Shaposhnikova_2021_Crystals_11_1052
PubMedID:
Gene_locus related to this paper: rhoso-halo1

Related information

Gene_locus rhoso-halo1
Structure rhoso-halo1    7O8B    7O3O

Citations formats

Shaposhnikova A, Kuty M, Chaloupkova R, Damborsky J, Smatanova IK, Minofar B, Prudnikova T (2021)
Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids
Crystals 11 :1052

Shaposhnikova A, Kuty M, Chaloupkova R, Damborsky J, Smatanova IK, Minofar B, Prudnikova T (2021)
Crystals 11 :1052