2BTE
Thermus thermophilus Leucyl-tRNA synthetase complexed with a tRNAleu transcript in the post-editing conformation and a post- transfer editing substrate analogue
Summary for 2BTE
| Entry DOI | 10.2210/pdb2bte/pdb |
| Related | 1H3N 1OBC 1OBH 2BYT |
| Descriptor | AMINOACYL-TRNA SYNTHETASE, TRNALEU TRANSCRIPT WITH ANTICODON CAG, ZINC ION, ... (9 entities in total) |
| Functional Keywords | ligase, class i aminoacyl-trna synthetase editing |
| Biological source | THERMUS THERMOPHILUS More |
| Total number of polymer chains | 4 |
| Total formula weight | 260229.93 |
| Authors | Cusack, S.,Tukalo, M.,Yaremchuk, A.,Fukunaga, R.,Yokoyama, S. (deposition date: 2005-05-31, release date: 2005-09-15, Last modification date: 2023-12-13) |
| Primary citation | Tukalo, M.,Yaremchuk, A.,Fukunaga, R.,Yokoyama, S.,Cusack, S. The Crystal Structure of Leucyl-tRNA Synthetase Complexed with tRNA(Leu) in the Post-Transfer- Editing Conformation. Nat.Struct.Mol.Biol., 12:923-, 2005 Cited by PubMed Abstract: Leucyl-tRNA synthetase (LeuRS) has a specific post-transfer editing activity directed against mischarged isoleucine and similar noncognate amino acids. We describe the post-transfer-editing and product complexes of Thermus thermophilus LeuRS (LeuRSTT) with tRNA(Leu) at 2.9- to 3.3-A resolution. In the post-transfer-editing configuration, A76 binds in the editing active site exactly as previously found for the adenosine moiety of a small-molecule editing-substrate analog. The 60 C-terminal residues of LeuRSTT, unseen in previous structures, fold into a compact domain flexibly linked to the rest of the molecule and interacting with the G19-C56 tertiary base pair of tRNA(Leu). LeuRS recognition of tRNA(Leu) depends essentially on tRNA shape rather than base-specific interactions. The structures show that considerable domain rotations, notably of the editing domain, accompany the tRNA-3' end dynamics associated successively with aminoacylation, post-transfer editing and product release. PubMed: 16155583DOI: 10.1038/NSMB986 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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