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 (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 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 | 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 | 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 | 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 |