Cloned (Comment) | Organism |
---|---|
expression of truncated enzyme SceTyrRS comprising residues 1-364 | 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 | Comment | Organism |
---|---|---|
additional information | construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS | Saccharomyces cerevisiae |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Saccharomyces cerevisiae |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P36421 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant truncated enzyme SceTyrRS comprising residues 1-364 | Saccharomyces cerevisiae |
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Comment | Organism |
---|---|---|
More | structural comparison of TyrRS of different origin, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Tyrosyl-tRNA synthetase | - |
Saccharomyces cerevisiae |
TyrRS | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |