1H3N
Leucyl-tRNA synthetase from Thermus thermophilus complexed with a sulphamoyl analogue of leucyl-adenylate
Summary for 1H3N
| Entry DOI | 10.2210/pdb1h3n/pdb |
| Descriptor | LEUCYL-TRNA SYNTHETASE, LEUCINE, [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDRO-2-FURANYL]METHYL SULFAMATE, ... (6 entities in total) |
| Functional Keywords | aminoacyl-trna synthetase, class i aminoacyl-trna synthetase, atp + l-leucine + trna (leu) -> amp + ppi + l-leucyl-trna(leu), ligase |
| Biological source | THERMUS THERMOPHILUS |
| Total number of polymer chains | 1 |
| Total formula weight | 102066.65 |
| Authors | Cusack, S.,Yaremchuk, A.,Tukalo, M. (deposition date: 2002-09-11, release date: 2002-09-27, Last modification date: 2024-05-08) |
| Primary citation | Cusack, S.,Yaremchuk, A.,Tukalo, M. The 2A Structure of Leucyl-tRNA Synthetase and its Complex with a Leucyl-Adenylate Analogue Embo J., 19:2351-, 2000 Cited by PubMed Abstract: Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large monomeric class I synthetases. Each contains a homologous insertion domain of approximately 200 residues, which is thought to permit them to hydrolyse ('edit') cognate tRNA that has been mischarged with a chemically similar but non-cognate amino acid. We describe the first crystal structure of a leucyl-tRNA synthetase, from the hyperthermophile Thermus thermophilus, at 2.0 A resolution. The overall architecture is similar to that of isoleucyl-tRNA synthetase, except that the putative editing domain is inserted at a different position in the primary structure. This feature is unique to prokaryote-like leucyl-tRNA synthetases, as is the presence of a novel additional flexibly inserted domain. Comparison of native enzyme and complexes with leucine and a leucyl- adenylate analogue shows that binding of the adenosine moiety of leucyl-adenylate causes significant conformational changes in the active site required for amino acid activation and tight binding of the adenylate. These changes are propagated to more distant regions of the enzyme, leading to a significantly more ordered structure ready for the subsequent aminoacylation and/or editing steps. PubMed: 10811626DOI: 10.1093/EMBOJ/19.10.2351 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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