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Literature summary extracted from

  • Sekine, S.; Shichiri, M.; Bernier, S.; Chenevert, R.; Lapointe, J.; Yokoyama, S.
    Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase (2006), Structure, 14, 1791-1799.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.1.1.17 tRNA GluRS is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation, tRNA serves as the enzyme activator in the first step, and as the substrate in the second step of aminoacylation, overview, On the other hand, the main chain of the glutamate is immature glutamate-binding site in the absence of tRNA Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.17 crystallization of complexes: 1. GluRS and L-Glu, 2. GluRS, tRNAGlu, and L-Glu, 3. GluRS, tRNAGlu, ATP, and L-glutamol, 4. GluRS, tRNAGlu, and L-glutamyl-sulfamoyl adenosine, by hanging drop vapour diffusion method, 5.0 mg/ml enzyme in 10 mM MOPS-Na buffer, pH 6.5, MgCl2, 5 mM 2-mercaptoethanol, 1% PEG 6000, and 2 mM L-glutamate, equilibration against a 1 ml reservoir solution containing 10% PEG at 4°C, ERS/tRNA/Glu and ERS/tRNA/ESA crystals are prepared by diffusing 1 mM L-glutamate and 0.5 mM glutamyl-sulfamoyl adenosine, i.e. ESA, respectively, into the ERS/tRNA binary complex crystals, ERS/tRNA/ATP/Eol crystals are obtained by adding both 1 mM ATP and 1 mM L-glutamol, i.e. Eol, to drops containing the ERS/tRNA binary complex, X-ray diffraction structure determination and analysis at 1.98 A, 2.4 A, 2.2 A, and 2.69 A resolution, respectively Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Mg2+
-
 Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu Thermus thermophilus
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Thermus thermophilus P27000
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu structural bases of transfer RNA-dependent L-glutamate recognition and activation by the enzyme, the glutamate-binding site is immature in the absence of tRNA, overview Thermus thermophilus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 additional information substrate and co-factor recognition and binding structures, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site, the collaborative site is functional, amino acid specificity is generated in the GluRS-tRNA complex, overview Thermus thermophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.17 More the pretransition-state quaternary complex, crystal structure analysis, in the GluRS-tRNAGlu-Glu structure, GluRS and tRNAGlu collaborate to form a highly complementary L-glutamate-binding site Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.17 GluRS
-
 Thermus thermophilus
6.1.1.17 Glutamyl-tRNA synthetase
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.17 ATP ATP binds to the 'productive' subsite, due to the tRNA-induced rearrangement of the binding site, which is, at least partially, the structural basis of the tRNA-dependent enzyme activation for amino acid activation Thermus thermophilus