Literature summary for 6.1.1.1 extracted from

Tsunoda, M.; Kusakabe, Y.; Tanaka, N.; Ohno, S.; Nakamura, M.; Senda, T.; Moriguchi, T.; Asai, N.; Sekine, M.; Yokogawa, T.; Nishikawa, K.; Nakamura, K.T.
Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms (2007), Nucleic Acids Res., 35, 4289-4300.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of truncated enzyme SceTyrRS comprising residues 1-364	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution

Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate	i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tyrosine + tRNATyr	Saccharomyces cerevisiae	-	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P36421	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant truncated enzyme SceTyrRS comprising residues 1-364	Saccharomyces cerevisiae

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr	reaction via reactive aminoacyl-adenylate intermediate, anticodon recognition mode and involved residues Tyr43, Asp177, Tyr170, Gln174 and Gln192, overview, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + L-tyrosine + tRNATyr	-	Saccharomyces cerevisiae	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?
ATP + L-tyrosine + tRNATyr	identitification of determinants in the cognate tRNATyr, the tRNATyr molecule forms an L-shaped structure, the acceptor stem and anticodon loop of the tRNATyr interact with different subunits of the dimeric TyrRS molecule, overview	Saccharomyces cerevisiae	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?
additional information	the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms, overview	Saccharomyces cerevisiae	?	-	?

Subunits

Subunits	Comment	Organism
More	structural comparison of TyrRS of different origin, overview	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
Tyrosyl-tRNA synthetase	-	Saccharomyces cerevisiae
TyrRS	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Saccharomyces cerevisiae