Literature summary for 6.1.1.17 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.

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Thermus thermophilus

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	P27000	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + L-glutamate + tRNAGlu	-	Thermus thermophilus	AMP + diphosphate + L-glutamyl-tRNAGlu	-	?
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	-	?
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

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
GluRS	-	Thermus thermophilus
Glutamyl-tRNA synthetase	-	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
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