Literature summary for 6.1.1.2 extracted from

Zhou, M.; Dong, X.; Shen, N.; Zhong, C.; Ding, J.
Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design (2010), Nucleic Acids Res., 38, 3399-3413.

Cloned(Commentary)

Cloned (Comment)	Organism
gene trpRS, expression of His-tagged TrpRS in Escherichia coli strain BL21(DE3)	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged TrpRS in apo form and in complexes with AMP, Trp, or TrpNH2O, the complexes contain a sulfate ion bound at the active site which mimics the alpha- or beta-phosphate group of ATP during tryptophan activation, hanging drop vapor diffusion method, 20°C, 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 5 mM 2-mercaptoethanol, and 1 mM PMSF, mixed with crystallization solutions, containing 0.1 M HEPES, pH 5.9, and 2.2 M (NH4)2SO4, with 0.0005 ml of 20 mM Trp or TrpNH2O for the Trp or TrpNH2O complexes, or with 100 mM ATP for the AMP complex, 2 days to 1 week, X-ray diffraction structure determination and analysis at 2.1-3.1 A resolution, modelling	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

purified recombinant His-tagged TrpRS in apo form and in complexes with AMP, Trp, or TrpNH2O, the complexes contain a sulfate ion bound at the active site which mimics the alpha- or beta-phosphate group of ATP during tryptophan activation, hanging drop vapor diffusion method, 20°C, 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 5 mM 2-mercaptoethanol, and 1 mM PMSF, mixed with crystallization solutions, containing 0.1 M HEPES, pH 5.9, and 2.2 M (NH4)2SO4, with 0.0005 ml of 20 mM Trp or TrpNH2O for the Trp or TrpNH2O complexes, or with 100 mM ATP for the AMP complex, 2 days to 1 week, X-ray diffraction structure determination and analysis at 2.1-3.1 A resolution, modelling

Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	Saccharomyces cerevisiae	-	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	gene trpS	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged TrpRS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	-	Saccharomyces cerevisiae	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?
ATP + L-tryptophan + tRNATrp	Trp and AMP binding structures, overview	Saccharomyces cerevisiae	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?

Subunits

Subunits	Comment	Organism
More	structure molecular modeling and dynamics simulation, overview	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
TrpRS	-	Saccharomyces cerevisiae
Tryptophanyl-tRNA synthetase	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
physiological function	specific activation of amino acids by aminoacyl-tRNA synthetases is essential for maintaining translational fidelity	Saccharomyces cerevisiae