Cloned (Comment) | Organism |
---|---|
expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
mutant mt-TyrRS-DS4, lacking the C-terminal S4-like domain, in complex with Tyr-AMS, an adenylate analogue, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
M252A | site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, tRNA mutant U73 is no more charged by mt-TyrRS upon Met252Ala mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Met252 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme | Homo sapiens |
Q202A | site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Gln202 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme | Homo sapiens |
S200A | site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, replacing Ser200 with Glu completely abolishes tyrosylation activity of wild-type and mutated tRNATyr transcripts | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | the mt-TyrRS is strictly mitochondrial, mitochondrial idiosyncrasies | Homo sapiens | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tyrosine + tRNATyr | Homo sapiens | - |
AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged full-length wild-type and mutant mitochondrial enzymes, and truncated mutant mt-TyrRS-DS4 mitochondrial enzyme from Escherichia coli by nickel affinity chromatography | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr | functional importance of Ser200 in the catalytic domain in line with an involvement of A73 rather than N1-N72 in tyrosine identity, active site structure, role of clusters 1 and 2 in tRNATyr acceptor arm | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tyrosine + tRNATyr | - |
Homo sapiens | AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimeric mitochondrial enzyme crystal structure analysis, the active mutant mitochondrial enzyme, deprived of the C-terminal S4-like domain, resembles eubacterial TyrRSs with a canonical tyrosine-binding pocket and adenylate-binding residues typical of class I synthetases, mt-TyrRS shows an asymmetry propagating from the dimer interface toward the two catalytic sites and extremities of each subunit, structure comparisons with other TyrRSs, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
mitochondrial tyrosyl-tRNA synthetase | - |
Homo sapiens |
mt-TyrRS | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens |