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Literature summary for 6.1.1.2 extracted from

  • Yang, X.L.; Otero, F.J.; Ewalt, K.L.; Liu, J.; Swairjo, M.A.; Koehrer, C.; RajBhandary, U.L.; Skene, R.J.; McRee, D.E.; Schimmel, P.
    Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis (2006), EMBO J., 25, 2919-2929.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified protein in complex with uncharged tRNA and aminoacylated tRNA in a 1:1 mixture, sitting drop vapour diffusion method, 0.002 ml of protein in 10 mM HEPES, pH 7.5, 20 mM KCl, 0.02% NaN3, and 2 mM 2-mercaptoethanol, addition of 230 mM of TrpRS, 250 mM of tRNATrp, 5 mM tryptophan and 10 mM AMP-PNP, mixed with 0.002 ml reservoir solution containing 2 M ammonium sulfate and 0.1 M HEPES pH 6.9, 4°C, X-ray diffraction structure determination and analysis at 2.9 A resolution, SAD method using a selenium-labeled crystal Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information preparation of alpha17 deletion mini-TrpRS, DELTAD382–Q389, by site-directed mutagensis, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-tryptophan + tRNATrp Homo sapiens
-
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P23381
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tryptophan + tRNATrp
-
Homo sapiens AMP + diphosphate + L-tryptophanyl-tRNATrp
-
?
ATP + L-tryptophan + tRNATrp tRNA substrate from Bos taurus, tryptophan binding pocket structure, overview, two distinct tRNA conformations: uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits, in this cross-dimer tRNA complex, the class I enzyme has a class II-like tRNA binding mode, the aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF-1a, suggesting that the product of aminoacylation can be directly handed off to EF-1alpha for the next step of protein synthesis, recognition mechanisms, overview Homo sapiens AMP + diphosphate + L-tryptophanyl-tRNATrp
-
?
additional information the enzyme interacts directly with elongation factor 1alpha, which carries charged tRNA to the ribosome Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More secondary structure determination and analysis, sequence comparisons, overview Homo sapiens

Synonyms

Synonyms Comment Organism
TrpRS
-
Homo sapiens
Tryptophanyl-tRNA synthetase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at, aminoacylation Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at, aminoacylation Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens