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Literature summary extracted from

  • Arnfors, L.; Hansen, T.; Schönheit, P.; Ladenstein, R.; Meining, W.
    Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal member of the ribokinase family (2006), Acta Crystallogr. Sect. D, 62, 1085-1097.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.B20 sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.B20 Mg2+ there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.B20 Methanocaldococcus jannaschii Q57849
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2.7.1.B20 Methanocaldococcus jannaschii DSM 2661 Q57849
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Synonyms

EC Number Synonyms Comment Organism
2.7.1.B20 MJ0406 locus name Methanocaldococcus jannaschii
2.7.1.B20 MjNK
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Methanocaldococcus jannaschii
2.7.1.B20 nucleoside kinase
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Methanocaldococcus jannaschii