3AFH
Crystal structure of Thermotoga maritima nondiscriminating glutamyl-tRNA synthetase in complex with a glutamyl-AMP analog
3AFH の概要
| エントリーDOI | 10.2210/pdb3afh/pdb |
| 分子名称 | Glutamyl-tRNA synthetase 2, O5'-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE (3 entities in total) |
| 機能のキーワード | protein-substrate complex, non-discriminating glutamyl-trna synthetase, aminoacyl-trna synthetase, atp-binding, ligase, nucleotide-binding, protein biosynthesis |
| 由来する生物種 | Thermotoga maritima |
| 細胞内の位置 | Cytoplasm: Q9X2I8 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 58001.03 |
| 構造登録者 | |
| 主引用文献 | Ito, T.,Kiyasu, N.,Matsunaga, R.,Takahashi, S.,Yokoyama, S. Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima Acta Crystallogr.,Sect.D, 66:813-820, 2010 Cited by PubMed Abstract: Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNA(Glu) only, while ND-GluRS glutamylates both tRNA(Glu) and tRNA(Gln). ND-GluRS produces the intermediate Glu-tRNA(Gln), which is converted to Gln-tRNA(Gln) by Glu-tRNA(Gln) amidotransferase. Two GluRS homologues from Thermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of the T. maritima ND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 A resolution. The T. maritima ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNA(Gln) by ND-GluRS was measured in the presence of the bacterial Glu-tRNA(Gln) amidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNA(Gln). PubMed: 20606262DOI: 10.1107/S0907444910019086 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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