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Literature summary extracted from

  • Drebes, J.; Perbandt, M.; Wrenger, C.; Betzel, C.
    Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus (2011), Acta Crystallogr. Sect. F, 67, 479-481.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.50 expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.50 enzyme with a phosphate ion occupying the position of the beta-phosphate of the nucleotide, mixing of 0.001 ml of protein solution containing 1.95 mg/ml protein in 20 mM Tris-HCl containing 200 mM NaCl and 1 mM DTT, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M CHESS buffer, pH 9.3, and 0.88 M sodium citrate as the precipitant, 20°C, 1 week, 25% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 1.85 A resolution Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.50 Pyrococcus horikoshii
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-
-
2.7.1.50 Pyrococcus horikoshii OT-3
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.50 recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by gel filtration, anion exchange chromatography to over 95% purity Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.50 additional information the active site is located at the interface between adjacent subunits. Each active site contains a thiazole-binding site and a nucleotide-binding site, structure, overview. Asp residue as a catalytic base Pyrococcus horikoshii ?
-
 ?
2.7.1.50 additional information the active site is located at the interface between adjacent subunits. Each active site contains a thiazole-binding site and a nucleotide-binding site, structure, overview. Asp residue as a catalytic base Pyrococcus horikoshii OT-3 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.50 More monomer structure, docking of ternary complexes, tertiary structure, molecular modelling, overview Pyrococcus horikoshii
2.7.1.50 trimer residues involved in hydrogen bonds between subunits in the enzyme trimer, overview Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
2.7.1.50 4-methyl-5-beta-hydroxyethylthiazole kinase
-
 Pyrococcus horikoshii
2.7.1.50 ThiK
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 Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
2.7.1.50 evolution three-quarters of the residues involved in interfacial regions are conserved, also the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK) Pyrococcus horikoshii
2.7.1.50 additional information the enzyme topology shows the typical ribokinase fold of an alpha/beta protein. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the trimeric quaternary association Pyrococcus horikoshii