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Literature summary for 6.1.1.3 extracted from

  • Shimizu, S.; Juan, E.C.; Miyashita, Y.I.; Sato, Y.; Hoque, M.M.; Suzuki, K.; Yogiashi, M.; Tsunoda, M.; Dock-Bregeon, A.C.; Moras, D.; Sekiguchi, T.; Takenaka, A.
    Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from Aeropyrum pernix and Sulfolobus tokodaii (2008), Acta Crystallogr. Sect. F, 64, 903-910.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
the two types of ThrRS from the crenarchaea Aeropyrum pernix and Sulfolobus tokodaii are overexpressed in Eschericha coli Aeropyrum pernix
the two types of ThrRS from the crenarchaea Aeropyrum pernix and Sulfolobus tokodaii are overexpressed in Eschericha coli Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized by the hanging-drop vapour diffusion method Aeropyrum pernix
crystallized by the hanging-drop vapour diffusion method Sulfurisphaera tokodaii
crystallized by the hanging-drop vapour diffusion method. Diffraction data are collected and the structure of a selenomethionine-labelled Aeropyrum pernix type-1 ThrRS crystal is solved using the multiple anomalous dispersion method Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30860
-
 predicted from cDNA Sulfurisphaera tokodaii
45000
-
 predicted from cDNA Aeropyrum pernix
53120
-
 predicted from cDNA Aeropyrum pernix
63110
-
 predicted from cDNA Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
 several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS
-
Sulfurisphaera tokodaii
-
 several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS
-

Subunits

Subunits Comment Organism
homodimer ApThrRS-1 forms a homodimer of subunits which are related to each other by crystallographic twofold rotation symmetry along the a axis. The amino-acid residues at the interface interact with each other through hydrogen bonds and van der Waals contacts between the two subunits. This structural feature is consistent with the dimer formation of the class II ThrRSscrystal structure Aeropyrum pernix
homodimer ApThrRS-2 might form a dimer between the editing domains, as the catalytic domain for dimerization is missing. This is consistent with the results of gel-filtration experiment, which shows that the molecular size of ApThrRS-2 is equivalent to twice that of the subunit Aeropyrum pernix

Synonyms

Synonyms Comment Organism
ApThrRS-1 protein contains the catalytic domain of ThrRS Aeropyrum pernix
ApThrRS-2 protein contains the editing domain of ThrRS Aeropyrum pernix
SfThrRS-1 protein contains the catalytic domain of ThrRS Sulfurisphaera tokodaii
SfThrRS-2 protein contains the editing domain of ThrRS Sulfurisphaera tokodaii
Threonyl-tRNA synthetase
-
 Aeropyrum pernix
Threonyl-tRNA synthetase
-
 Sulfurisphaera tokodaii