Literature summary for 2.7.1.164 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
D146A	mutant is active in vivo	Methanocaldococcus jannaschii
K142A	mutant is active in vivo	Methanocaldococcus jannaschii
K142A/Y143A	mutant shows severely reduced activity with the Methanopyrus kandleri tRNASec substrate	Methanocaldococcus jannaschii
K17A	mutation abolishes catalytic activity and and inhibits tRNASec recognition	Methanocaldococcus jannaschii
K30A	mutant is defective in phosphorylation activity	Methanocaldococcus jannaschii
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
N161A	mutant is defective in phosphorylation activity	Methanocaldococcus jannaschii
S18A	mutation abolishes catalytic activity and and inhibits tRNASec recognition	Methanocaldococcus jannaschii
W145A	mutant is active in vivo	Methanocaldococcus jannaschii

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q58933	-	-
Methanocaldococcus jannaschii DSM 2661	Q58933	-	-