1H3F
Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with tyrosinol
Summary for 1H3F
| Entry DOI | 10.2210/pdb1h3f/pdb |
| Related | 1H3E |
| Descriptor | TYROSYL-TRNA SYNTHETASE, SULFATE ION, 4-[(2S)-2-amino-3-hydroxypropyl]phenol, ... (4 entities in total) |
| Functional Keywords | ligase, aminoacyl-trna synthetase, atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase |
| Biological source | THERMUS THERMOPHILUS |
| Total number of polymer chains | 2 |
| Total formula weight | 98387.13 |
| Authors | Cusack, S.,Yaremchuk, A.,Kriklivyi, I.,Tukalo, M. (deposition date: 2002-08-28, release date: 2002-09-12, Last modification date: 2024-05-01) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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