Crystallization (Comment) | Organism |
---|---|
purified TrpRS, grown at room temperature by vapor equilibration from sitting drops containing 0.002 ml of protein solution containing 11 mg/ml protein, 500 mM NaCl, 20 mM HEPES, 2 mM BME, 5% glycerol, 0.025% NaAzide, pH 7.5, mixed with 0.001 ml of crystallization buffer containing 2.7 M ammonium sulfate, 5 mM DTT, 0.1 M citric acid, pH 5.2, X-ray diffraction structure determination and analysis at 2.1 A resolution | Giardia intestinalis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Giardia intestinalis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tryptophan + tRNATrp | Giardia intestinalis | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Giardia intestinalis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tryptophan + tRNATrp | - |
Giardia intestinalis | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
ATP + L-tryptophan + tRNATrp | the active site is located in a deep, long pocket within the catalytic domain, and is surrounded by several conserved features | Giardia intestinalis | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
additional information | modeling of probable tRNA binding, overview | Giardia intestinalis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | (alpha2)2 homotetramer, crystal structure analysis, the N-terminus forms a 16-residue a-helix, structure modelling, overview. The typical class I aminoacyl-tRNA synthetase contains an N-terminal extension, residues 1-64, a Rossman-fold catalytic domain, residues 65-324, 415-429, and an anticodon recognition domain, residues 325-414 | Giardia intestinalis |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the class I aminoacyl-tRNA synthetases | Giardia intestinalis |
TrpRS | - |
Giardia intestinalis |
Tryptophanyl-tRNA synthetase | - |
Giardia intestinalis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | the ATP-binding site, a loop formed by the residues 311-315 of the KMSAS motif, is sandwiched by the characteristic class I HIGH motif, residues 84-87, and by residues 272-275 of a GIEQ motif that is weakly conserved among TrpRS sequences | Giardia intestinalis |
General Information | Comment | Organism |
---|---|---|
evolution | the activation reaction mechanism of TrpRS from the basal eukaryote Gardia lamblia differs from that of higher eukaryotes, overview. The N-terminus of the class I aminoacyl-tRNA synthetase from Gardia lamblia forms a 16-residue alpha-helix. This helix replaces a beta-hairpin that is required by human TrpRS for normal activity and infers to play a similar role in all eukaryotic TrpRS | Giardia intestinalis |