1H3F
Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with tyrosinol
1H3F の概要
エントリーDOI | 10.2210/pdb1h3f/pdb |
関連するPDBエントリー | 1H3E |
分子名称 | TYROSYL-TRNA SYNTHETASE, SULFATE ION, 4-[(2S)-2-amino-3-hydroxypropyl]phenol, ... (4 entities in total) |
機能のキーワード | ligase, aminoacyl-trna synthetase, atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase |
由来する生物種 | THERMUS THERMOPHILUS |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 98387.13 |
構造登録者 | Cusack, S.,Yaremchuk, A.,Kriklivyi, I.,Tukalo, M. (登録日: 2002-08-28, 公開日: 2002-09-12, 最終更新日: 2024-05-01) |
主引用文献 | Yaremchuk, A.,Kriklivyi, I.,Tukalo, M.,Cusack, S. Class I Tyrosyl-tRNA Synthetase Has a Class II Mode or tRNA Recognition Embo J., 21:3829-, 2002 Cited by PubMed Abstract: Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem. PubMed: 12110594DOI: 10.1093/EMBOJ/CDF373 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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