Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Angstroms resolution: an enzyme catalyst generated via adaptive mutation

The three-dimensional structure of 4-chlorobenzoyl-CoA dehalogenase from Pseudomonas sp. strain CBS-3 is studied. Crystallographic analysis showed that the enzyme is a trimer and each subunit folds into two distinct motifs. The bigger, N-terminal domain has 10 strands of beta-pleated sheet that form two distinct layers which are almost perpendicular to each other. Alpha-helices are found on the sides of the layers of beta-sheet. The C-terminal domain is made of three amphiphilic alpha-helices. The two domains of the subunit are linked by a cation.