Literature summary for 6.1.1.1 extracted from

Turner, J.M.; Graziano, J.; Spraggon, G.; Schultz, P.G.
Structural plasticity of an aminoacyl-tRNA synthetase active site (2006), Proc. Natl. Acad. Sci. USA, 103, 6483-6488.

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis of two enzymes types, expression of tyrosyl aminoacyl-tRNA synthetase as C-terminally His6-tagged enzyme in Escherichia coli	Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20°C or 4°C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution	Methanocaldococcus jannaschii

Crystallization (Comment)

Organism

purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20°C or 4°C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution

Methanocaldococcus jannaschii

Protein Variants

Protein Variants	Comment	Organism
additional information	structural comparison of wild-type enzyme and naturally occuring mutant variant p-BrPhe TyrRSs, the latter shows an altered substrate specificity charging 4-bromophenylalanine, 3-(2-naphthyl)alanine, or 4-acetylphenylalanine, overview	Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
ATP + 3-(2-naphthyl)alanine + tRNATyr	Methanocaldococcus jannaschii	activity of a natural mutant enzyme, NpAla TyrRS activity	AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr	-	?
ATP + 4-acetylphenylalanine + tRNATyr	Methanocaldococcus jannaschii	activity of a natural mutant enzyme	AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr	-	?
ATP + 4-bromophenylalanine + tRNATyr	Methanocaldococcus jannaschii	activity of a natural mutant enzyme, p-BrPhe TyrRS activity	AMP + diphosphate + 4-bromophenylalanyl-tRNATyr	-	?
ATP + L-tyrosine + tRNATyr	Methanocaldococcus jannaschii	wild-type activity	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q57834	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase from Escherichia coli by nickel affinity and ion exchange chromatography to homogeneity	Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + 3-(2-naphthyl)alanine + tRNATyr	activity of a natural mutant enzyme, NpAla TyrRS activity	Methanocaldococcus jannaschii	AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr	-	?
ATP + 3-(2-naphthyl)alanine + tRNATyr	activity of a natural mutant enzyme, NpAla TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site	Methanocaldococcus jannaschii	AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr	-	?
ATP + 4-acetylphenylalanine + tRNATyr	activity of a natural mutant enzyme	Methanocaldococcus jannaschii	AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr	-	?
ATP + 4-acetylphenylalanine + tRNATyr	activity of a natural mutant enzyme, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site	Methanocaldococcus jannaschii	AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr	-	?
ATP + 4-bromophenylalanine + tRNATyr	activity of a natural mutant enzyme, p-BrPhe TyrRS activity	Methanocaldococcus jannaschii	AMP + diphosphate + 4-bromophenylalanyl-tRNATyr	-	?
ATP + 4-bromophenylalanine + tRNATyr	activity of a natural mutant enzyme, p-BrPhe TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site	Methanocaldococcus jannaschii	AMP + diphosphate + 4-bromophenylalanyl-tRNATyr	-	?
ATP + L-tyrosine + tRNATyr	wild-type activity	Methanocaldococcus jannaschii	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?
additional information	high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview	Methanocaldococcus jannaschii	?	-	?

Synonyms

Synonyms	Comment	Organism
NpAla TyrRS	-	Methanocaldococcus jannaschii
p-BrPhe TyrRS	-	Methanocaldococcus jannaschii
tyrosyl aminoacyl-tRNA synthetase	-	Methanocaldococcus jannaschii
TyrRS	-	Methanocaldococcus jannaschii

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Methanocaldococcus jannaschii