Literature summary for 6.1.1.3 extracted from

Torres-Larios, A.; Sankaranarayanan, R.; Rees, B.; Dock-Bregeon, A.C.; Moras, D.
Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase (2003), J. Mol. Biol., 331, 201-211.

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Staphylococcus aureus

Crystallization (Comment)

Organism

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

Staphylococcus aureus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-threonine + tRNAThr	Staphylococcus aureus	-	AMP + diphosphate + L-threonyl-tRNAThr	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	Q8NW68	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli	Staphylococcus aureus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr	substrate binding and mechanism	Staphylococcus aureus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-threonine + tRNAThr	-	Staphylococcus aureus	AMP + diphosphate + L-threonyl-tRNAThr	-	?
ATP + L-threonine + tRNAThr	substrate binding induces conformational changes	Staphylococcus aureus	AMP + diphosphate + L-threonyl-tRNAThr	-	?

Synonyms

Synonyms	Comment	Organism
Synthetase, threonyl-transfer ribonucleate	-	Staphylococcus aureus
Threonine translase	-	Staphylococcus aureus
Threonine--tRNA ligase	-	Staphylococcus aureus
Threonine-transfer ribonucleate synthetase	-	Staphylococcus aureus
Threonyl-ribonucleic synthetase	-	Staphylococcus aureus
Threonyl-transfer ribonucleate synthetase	-	Staphylococcus aureus
Threonyl-transfer ribonucleic acid synthetase	-	Staphylococcus aureus
Threonyl-transfer RNA synthetase	-	Staphylococcus aureus
Threonyl-tRNA synthetase	-	Staphylococcus aureus
ThrRS	-	Staphylococcus aureus
TRS	-	Staphylococcus aureus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.7	-	assay at	Staphylococcus aureus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Staphylococcus aureus