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Literature summary extracted from

  • Araiso, Y.; Sherrer, R.L.; Ishitani, R.; Ho, J.M.; Söll, D.; Nureki, O.
    Structure of a tRNA-dependent kinase essential for selenocysteine decoding (2009), Proc. Natl. Acad. Sci. USA, 106, 16215-16220.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.164 sitting drop vapor diffusion method at 20°C, the structures of MjPSTK complexed with ADP and AMPPNP revealed that this enzyme belongs to the P-loop kinase class, and that the kinase domain is closely related to gluconate kinase and adenylate kinase. ATP is bound by the P-loop domain (residues 11-18). Formed by antiparallel dimerization of two O-phosphoseryl-tRNASec kinase monomers, the enzyme structure shows a deep groove with positive electrostatic potential. Located in this groove is the active site of the enzyme, which biochemical and genetic data suggest is composed of Asp-41, Arg-44, Glu-55, Tyr-82, Tyr-83, Met-86, and Met-132 Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.164 Methanocaldococcus jannaschii Q58933
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2.7.1.164 Methanocaldococcus jannaschii DSM 2661 Q58933
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.164
-
 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.7.1.164 O-phosphoseryl-tRNA(Sec) kinase
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 Methanocaldococcus jannaschii
2.7.1.164 PSTK
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 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
2.7.1.164 physiological function the enzyme is involved in the biosynthesis of selenocysteine Methanocaldococcus jannaschii