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6.1.1.3: threonine-tRNA ligase

This is an abbreviated version!
For detailed information about threonine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.3

Reaction

ATP
+
L-threonine
 +
tRNAThr
=
AMP
 +
diphosphate
 +
L-threonyl-tRNAThr

Synonyms

ApThrRS-1, ApThrRS-2, BaThrRS, EcThrRS, ectRNAThr, McThrRS, mitochondrial threonyl-tRNA synthetase, MJ1197, MmThrRS, More, Mst1, ScmtThrRS, SfThrRS-1, SfThrRS-2, Synthetase, threonyl-transfer ribonucleate, TarS, Thr-tRNA synthetase, Threonine translase, Threonine--tRNA ligase, Threonine-transfer ribonucleate synthetase, threonyl tRNA synthetase, Threonyl-ribonucleic synthetase, Threonyl-transfer ribonucleate synthetase, Threonyl-transfer ribonucleic acid synthetase, Threonyl-transfer RNA synthetase, Threonyl-tRNA synthetase, ThrRS, ThrRS1, ThrS, TRS

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.3 threonine-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.3 - threonine-tRNA ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapour diffusion method
-
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
-
the structure of ApThrRS-1 is determined at 2.3 A resolution
hanging drop vapor diffusion method, using 12% (w/v) PEG 4000, 21% (v/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.9
-
crystal structure, PDB code 1EVL, at 1.55 A resolution used for reaction mechanism analysis and molecular modeling
enzyme core DELTAN complexed with the essential operator domain mRNA, precipitation with 1.9 M ammonum sulfate in sodium cacodylate, pH 6.6, 4°C from solution containing 0.088 mM enzyme mutant DELTAN, 0.2 mM operator mRNA domain 2, 10 mM MgCl2, 10 mM substrate analogue 5'-O-(N-(L-threonyl)-sulfamoyl)adenosine, crystals are soaked in 25% v/v glycerol, X-ray diffraction structure determination at 3.6 A resolution and structure analysis
enzyme in complex with tRNAThr, hanging drop method, pH 6.5, solution containing ammonium acetate, ATP, and PEG 4000 as precipitant, X-ray diffraction structure determination at 2.9 A resolution and analysis
-
hanging drop vapor diffusion method, using 12% (w/v) PEG 4000, 21% (v/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.9
-
lamdaN-threonine-tRNA ligase complexed with Ser-AMS, X-ray diffraction structure determination at 1.65 A resolution and analysis
-
purified recombinant N-terminal part of the enzyme, i.e. N1 and N2 domains comprising residues 1-65 and 66-225 in one fragment, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modeling
X-ray structure determination at 2.9 A resolution, structure analysis of the wild-type enzyme and truncated mutant lamdaN in complex with L-threonine and L-serine
hanging drop vapor diffusion method, using 12% (w/v) PEG 4000, 21% (v/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.9
purified recombinant D-aminoacyl-tRNA deacylase-like domain with bound Ser3AA, hanging drop vapor diffusion method, mixing of equal volumes of protein, ligand and reservoir solution, crystallization from 0.2 M (NH4)2SO4, 0.1 M sodium cacodylate, pH 6.5, and 30% PEG 8000 and 0.1 M HEPES, pH 7.0, and 25% PEG 3350, purified recombinant D-aminoacyl-tRNA deacylase-like domain with bound SerAMS, using 0.1 M Bis-Tris, pH 6.5, and 25% PEG 3350, and the serine Pab-NTD–L-serine cocrystals from 0.1 M HEPES pH 7.0 and 25% PEG 8000, X-ray diffraction structure determination and analysis at 1.86-2.25 A resolution, overview
purified ultrafiltrated recombinant residues 1-183, hanging drop vapour diffusion method, protein solution, containing 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl, drops of varying volumes against 0.75 ml reservoir solution, at room temperature or at 4°C, preliminary X-ray diffraction for structure determination at 1.95 A resolution
-
complexed with an analog of Ser-AMP, sitting drop vapor diffusion method, using 0.1 M Na2HPO4/KH2PO4 (pH 6.2), 0.2 M NaCl, 10% (w/v) PEG 8000
-
enzyme complexed with ATP and threonine and complexed with substrate analogue 5'-O-(N-(L-threonyl)-sulfamoyl)adenosine, hanging drop method, 15 mg/ml protein in 20 mM HEPES, pH 7.2, 2 mM MgCl2, 100 mM KCl, in a 1:1:1 mixture with ligand solution containing 10 mM MgCl2, 10 mM ATP or 1 mM Thr-AMS, and well solution containing 50 mM Tris-HCl, pH 7.5-8.5, PEG 8000 12-14% w/v, and ammonium acetate or potassium chloride in the range 0.2-0.4 M, 2-3 days at 4°C, X-ray diffraction structure determination at resolution 2.8-3.2 A, structure analysis, modeling
crystallized by the hanging-drop vapour diffusion method
-
enzyme overproduced in Escherichia coli
-
hanging drop vapor diffusion method, using 12% (w/v) PEG 4000, 21% (v/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.9
-