A novel structurally characterized haloacid dehalogenase superfamily phosphatase from Thermococcus thioreducens with diverse substrate specificity

This study focuses on a new hypothetical HAD phosphatase from Thermococcus thioreducens. The protein crystallized in space group P21212, with unit-cell parameters a = 66.3, b = 117.0, c = 33.8   Å , and the crystals contained one molecule in the asymmetric unit. The protein structure was determined by X-ray crystallography and was refined to 1.75   Å resolution. The structure revealed a putative active site common to all HAD members. Computational docking into the crystal structure was used to propose substrates of the enzyme. The activity of this thermophilic enzyme towards several of the selected substrates was confirmed at temperatures of 37 ° C as well as 60 ° C.

Source: Acta Crystallographica Section D - July 29, 2019 Category: Biochemistry Authors: Havlickova, P. Brinsa, V. Brynda, J. Pachl, P. Prudnikova, T. Mesters, J.R. Kascakova, B. Kuty, M. Pusey, M.L. Ng, J.D. Rezacova, P. Kuta Smatanova, I. Tags: HAD superfamily hypothetical phosphatase crystal structure docking phosphatase assay research papers Source Type: research