6IAH

Phosphatase Tt82 from Thermococcus thioreducens

Summary for 6IAH

• Entry DOI: 10.2210/pdb6iah/pdb
• Descriptor: Hydrolase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: had superfamily, hypothetical phosphatase, docking, phosphatase assay, hydrolase
• Biological source: Thermococcus thioreducens
• Total number of polymer chains: 1
• Total formula weight: 28135.64

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.,Smatanova, I.K. (deposition date: 2018-11-26, release date: 2019-08-14, Last modification date: 2024-05-01)

Primary citation

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.,Smatanova, I.K.
A novel structurally characterized haloacid dehalogenase superfamily phosphatase from Thermococcus thioreducens with diverse substrate specificity.
Acta Crystallogr D Struct Biol, 75:743-752, 2019

PubMed Abstract: The haloacid dehalogenase (HAD) superfamily is one of the largest known groups of enzymes and the majority of its members catalyze the hydrolysis of phosphoric acid monoesters into a phosphate ion and an alcohol. Despite the fact that sequence similarity between HAD phosphatases is generally very low, the members of the family possess some characteristic features, such as a Rossmann-like fold, HAD signature motifs or the requirement for Mg ion as an obligatory cofactor. This study focuses on a new hypothetical HAD phosphatase from Thermococcus thioreducens. The protein crystallized in space group P222, 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.

PubMed: 31373573
DOI: 10.1107/S2059798319009586

Experimental method

X-RAY DIFFRACTION (1.75 Å)