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1.14.14.21: dibenzothiophene monooxygenase

This is an abbreviated version!
For detailed information about dibenzothiophene monooxygenase, go to the full flat file.

Word Map on EC 1.14.14.21

Reaction

dibenzothiophene
+ 2 FMNH2 + 2 O2 =
dibenzothiophene-5,5-dioxide
 + 2 FMN + 2 H2O

Synonyms

BdsC, benzothiophene monooxygenase, BT monooxygenase, cofactor-requiring dibenzothiophene monooxygenase, DBT monooxygenase, DBT-MO, DBT-monooxygenase, dibenzothiophene monooxygenase, dszC, TdsC

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.21 dibenzothiophene monooxygenase

Crystallization

Crystallization on EC 1.14.14.21 - dibenzothiophene monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme DszC, hanging drop vapour diffusion method, using a reservoir suliton containing 30% polyethylene glycol, 0.1 M sodium citrate, pH 5.6, and 0.2 M ammonium acetate, 4°C, X-ray diffraction structure determination and analysis
purified recombinant His-taged enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 20 mg/ml protein in 20 mM Tris-HCl (pH 8.0) and 150 mM NaCl, with FMN in a 1:10 molar ratio, with 0.002 ml of reservoir solution containing 200 mM lithium sulfate, 100 mM Bis-Tris, pH 6.5, and 35% w/v PEG 3350, equilibration against 0.3 ml reservoir solution, 4°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement using DszC structure, PDB ID 4JEK, as the search model
-
purified recombinant His-tagged enzyme in apoform and as FMN-bound enzyme DszC, two distinct conformations occur in the loop region (residues 131-142) adjacent to the active site, sitting drop vapor diffusion method, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution consisting of 0.2 M malonate, pH 6.0, 24% w/v PEG 3350, and 50 mM NaF, at 20°C, with or without 1 mM FMN, X-ray diffraction structure determination and analysis at 2.11 A an 2.3 A resolution, respectively, Each crystal contains two tetramers in the asymmetric unit, formed by two homodimers
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging-drop vapour-diffusion method, mixing of 10 mg/ml wild-type enzyme in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl with reservoir solution containing 17.5% PEG 3350, 200 mM Bis-Tris, pH 7.5, and 200 mM ammonium sulfate, and mixing of 5 mg/ml selenomethionine-labeled enzyme in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl with reservoir solution containing 25% PEG 3350, 100 mM PIPES, pH 7.0, 200 mM ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 2.4-2.9 A resolution
purified recombinant wild-type, selenomethionine-labeled, and mutant enzymes, hanging drop vapor diffusion method, mixing of 15-20 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 100 mM NaCl with an equal volume of reservoir solution containing 0.2 M L2SO4, 0.1 M Bis-Tris, pH 6.5, and 23% w/v PEG 3350, at 20°C, X-ray diffraction structure determination and analysis at 1.79 A resolution, molecular replacement and modelling