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Literature summary extracted from

  • Sherrer, R.L.; Araiso, Y.; Aldag, C.; Ishitani, R.; Ho, J.M.; Soell, D.; Nureki, O.
    C-terminal domain of archaeal O-phosphoseryl-tRNA kinase displays large-scale motion to bind the 7-bp D-stem of archaeal tRNA(Sec) (2011), Nucleic Acids Res., 39, 1034-1041.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.164 expression in Escherichia coli Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.164 in complex with an anticodon-stem/loop truncated tRNASec, to 2.4 A resolution. Truncated tRNASec is bound between the enzyme's C-terminal domain CTD and N-terminal kinase domain NTD that are connected by a flexible 11 amino acid linker. Upon tRNASec recognition, the CTD undergoes a 62-A movement to allow proper binding of the 7-bp D-stem. This large reorganization of the quaternary structure likely provides a means by which the unique tRNASec species can be accurately recognized with high affinity by the translation machinery Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.164 D146A mutant is active in vivo Methanocaldococcus jannaschii
2.7.1.164 K142A mutant is active in vivo Methanocaldococcus jannaschii
2.7.1.164 K142A/Y143A mutant shows severely reduced activity with the Methanopyrus kandleri tRNASec substrate Methanocaldococcus jannaschii
2.7.1.164 K17A mutation abolishes catalytic activity and and inhibits tRNASec recognition Methanocaldococcus jannaschii
2.7.1.164 K30A mutant is defective in phosphorylation activity Methanocaldococcus jannaschii
2.7.1.164 additional information truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity Methanocaldococcus jannaschii
2.7.1.164 N161A mutant is defective in phosphorylation activity Methanocaldococcus jannaschii
2.7.1.164 S18A mutation abolishes catalytic activity and and inhibits tRNASec recognition Methanocaldococcus jannaschii
2.7.1.164 W145A mutant is active in vivo 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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