Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Thermotoga maritima |
TM1875, sequence comparisons, expression in Escherichia coli strain Rosetta2(DE3) | Thermotoga maritima |
Crystallization (Comment) | Organism |
---|---|
the crystal structure of the Thermotoga maritima ND-GluRS, TM1875, is determined in complex with a Glu-AMP analogue at 2.0 A resolution. ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain | Thermotoga maritima |
TM1875 in complex with a Glu-AMP analogue, mixing of 0.0018 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 7.0, containing 5 mM MgCl2, 10 mM 2-mercaptoethanol, 50 mM NaCl, and 1 mM L-glutamylsulfamoyl adenosine, with 0.0018 ml reservoir solution containing 100 mM HEPES-NaOH, pH 7.5, 8% ethylene glycol and 15% PEG 8000, and 0.0004 ml of 30% D-sorbitol, equilibration against 0.5 ml reservoir solution, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution | Thermotoga maritima |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Thermotoga maritima | |
Mg2+ | required | Thermotoga maritima |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Thermotoga maritima | ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9X2I8 | - |
- |
Thermotoga maritima | Q9X2I8 | TM1875 | - |
Purification (Comment) | Organism |
---|---|
recombinant TM1875 from Escherichia coli strain Rosetta2 (DE3) by anion exchange chromatography and gel filtration | Thermotoga maritima |
using ion-exchange column chromatography and gel-filtration | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + Glu + tRNAGln | the glutamylation ability of tRNAGln by ND-GluRS is measured in the presence of the bacterial Glu-tRNAGln amidotransferase GatCAB. Glutamylation efficiency is not affected even in the presence of excess GatCAB | Thermotoga maritima | AMP + diphosphate + L-glutamyl-tRNAGln | - |
? | |
additional information | ND-GluRS TM1875 glutamylates both tRNAGlu and tRNAGln | Thermotoga maritima | ? | - |
? | |
additional information | TM1875 glutamylates both the tRNAGlu and tRNAGln transcripts | Thermotoga maritima | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | Thermotoga maritima ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain, structure, overview | Thermotoga maritima |
Synonyms | Comment | Organism |
---|---|---|
Glutamyl-tRNA synthetase | - |
Thermotoga maritima |
ND-GluRS | - |
Thermotoga maritima |
nondiscriminating GluRS | - |
Thermotoga maritima |
nondiscriminating glutamyl-tRNA synthetase | - |
Thermotoga maritima |
TM1875 | - |
Thermotoga maritima |
TM1875 | only TM1875 functions as a nondiscriminating GluRS | Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Thermotoga maritima |
General Information | Comment | Organism |
---|---|---|
physiological function | ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGln by Glu-tRNAGln amidotransferase. GluRS avoids competition with Glu-tRNAGln amidotransferase GatCAB and glutamylates tRNAGln | Thermotoga maritima |