We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.
        
Representative scheme of Haloalkane_dehalogenase-HLD2 structure and an image from PDBsum server
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3SK0 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
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3SK0Fold classification based on Structure-Structure alignment of Proteins - FSSP server