Literature summary for 6.1.1.1 extracted from

Yaremchuk, A.; Kriklivyi, I.; Tukalo, M.; Cusack, S.
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition (2002), EMBO J., 21, 3829-3840.

Crystallization (Commentary)

Crystallization (Comment)	Organism
pure enzyme, 12 mg/ml, or in complex with tyrosinol, hanging drop vapour diffusion technique, equal volumes of protein and a reservoir solution that contains 1.2 M ammonium sulfate, 10 mM MgCl2, 0.5 mM dithiothreitol, 50 mM MES, pH 5.8, X-ray diffraction structure determination and analysis, enzyme in complex with tyrosinol, ATP and tRNATyr, at 293K, equilibration of 0.004 ml protein-RNA solution against 1 ml reservoir solution, protein-RNA solution: 4-5 mg/ml of enzyme in a molar ratio of 1:1 or 1:2 with RNA, 5 mM tyrosinol, 10 mg MgCl2, 10 mM ATP, 50 mM HEPES, pH 7.0, 0.8 M ammonium sulfate, reservoir solution: 1.5-1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, 2-4 weeks, X-ray diffraction structure determination at 2.0-2.1 A resolution and analysis	Thermus thermophilus

Crystallization (Comment)

Organism

pure enzyme, 12 mg/ml, or in complex with tyrosinol, hanging drop vapour diffusion technique, equal volumes of protein and a reservoir solution that contains 1.2 M ammonium sulfate, 10 mM MgCl2, 0.5 mM dithiothreitol, 50 mM MES, pH 5.8, X-ray diffraction structure determination and analysis, enzyme in complex with tyrosinol, ATP and tRNATyr, at 293K, equilibration of 0.004 ml protein-RNA solution against 1 ml reservoir solution, protein-RNA solution: 4-5 mg/ml of enzyme in a molar ratio of 1:1 or 1:2 with RNA, 5 mM tyrosinol, 10 mg MgCl2, 10 mM ATP, 50 mM HEPES, pH 7.0, 0.8 M ammonium sulfate, reservoir solution: 1.5-1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, 2-4 weeks, X-ray diffraction structure determination at 2.0-2.1 A resolution and analysis

Thermus thermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + tyrosine + tRNATyr	Thermus thermophilus	-	AMP + Tyr-tRNATyr + diphosphate	-	?
ATP + tyrosine + tRNATyr	Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039	-	AMP + Tyr-tRNATyr + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	purified recombinant enzyme	-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039	-	purified recombinant enzyme	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr	mechanism, class I enzyme has a class II mode of cognate tRNA recognition	Thermus thermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + tyrosine + tRNATyr	-	Thermus thermophilus	AMP + Tyr-tRNATyr + diphosphate	-	?
ATP + tyrosine + tRNATyr	tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases	Thermus thermophilus	AMP + Tyr-tRNATyr + diphosphate	-	?
ATP + tyrosine + tRNATyr	-	Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039	AMP + Tyr-tRNATyr + diphosphate	-	?
ATP + tyrosine + tRNATyr	tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases	Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039	AMP + Tyr-tRNATyr + diphosphate	-	?

Subunits

Subunits	Comment	Organism
More	in the complex of enzyme and substrates, e.g. tRNATyr, the C-terminal domain of the enzyme is stabilized by binding in the elbow between the long variable arm and the anti-codon stem, and the linker peptide connecting it to the last helix of the alpha-helical domain becomes ordered	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
Tyrosyl-tRNA synthetase	-	Thermus thermophilus
TyrRS	-	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Thermus thermophilus