9SFQ
Structure at 1.9 A resolution of Thermus thermophilus tyrosyl-tRNA synthetase bound to wild-type tRNATyr(GUC).
This is a non-PDB format compatible entry.
Summary for 9SFQ
| Entry DOI | 10.2210/pdb9sfq/pdb |
| Descriptor | Tyrosine--tRNA ligase, Wild-type, fully modified Thermus thermopilus tRNATyr(GUC), SULFATE ION, ... (7 entities in total) |
| Functional Keywords | aminoacyl-trna synthetase, ligase, aminoacyl-adenylate, rna binding protein |
| Biological source | Thermus thermophilus HB27 More |
| Total number of polymer chains | 2 |
| Total formula weight | 79060.26 |
| Authors | Cusack, S. (deposition date: 2025-08-20, release date: 2025-09-24, Last modification date: 2025-12-10) |
| Primary citation | Yaremchuk, A.,Kriklivyi, I.,Tukalo, M.,Cusack, S. Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J, 21:3829-3840, 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 (1.89 Å) |
Structure validation
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