1F7V
CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG
Summary for 1F7V
| Entry DOI | 10.2210/pdb1f7v/pdb |
| Related | 1BS2 1F7U |
| Descriptor | TRNA(ARG), ARGINYL-TRNA SYNTHETASE (3 entities in total) |
| Functional Keywords | trna-protein complex, aminoacylation, arginyl-trna synthetase, ligase-rna complex, ligase/rna |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 94191.64 |
| Authors | Delagoutte, B.,Moras, D.,Cavarelli, J. (deposition date: 2000-06-28, release date: 2001-06-27, Last modification date: 2024-02-07) |
| Primary citation | Delagoutte, B.,Moras, D.,Cavarelli, J. tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding EMBO J., 19:5599-5610, 2000 Cited by PubMed Abstract: The 2.2 A crystal structure of a ternary complex formed by yeast arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the L-arginine substrate highlights new atomic features used for specific substrate recognition. This first example of an active complex formed by a class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA illustrates additional strategies used for specific tRNA selection. The enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop never seen before. Moreover, the anticodon binding triggers conformational changes in the catalytic center of the protein. The comparison with the 2.9 A structure of a binary complex formed by yeast arginyl-tRNA synthetase and tRNA(Arg) reveals that L-arginine binding controls the correct positioning of the CCA end of the tRNA(Arg). Important structural changes induced by substrate binding are observed in the enzyme. Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction. PubMed: 11060012DOI: 10.1093/emboj/19.21.5599 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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