1N9W
Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus
Summary for 1N9W
| Entry DOI | 10.2210/pdb1n9w/pdb |
| Descriptor | aspartyl-tRNA synthetase 2 (2 entities in total) |
| Functional Keywords | biosynthetic protein |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 96794.52 |
| Authors | Charron, C.,Roy, H.,Blaise, M.,Giege, R.,Kern, D. (deposition date: 2002-11-26, release date: 2003-04-08, Last modification date: 2024-02-14) |
| Primary citation | Charron, C.,Roy, H.,Blaise, M.,Giege, R.,Kern, D. Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain EMBO J., 22:1632-1643, 2003 Cited by PubMed Abstract: In most organisms, tRNA aminoacylation is ensured by 20 aminoacyl-tRNA synthetases (aaRSs). In eubacteria, however, synthetases can be duplicated as in Thermus thermophilus, which contains two distinct AspRSs. While AspRS-1 is specific, AspRS-2 is non-discriminating and aspartylates tRNA(Asp) and tRNA(Asn). The structure at 2.3 A resolution of AspRS-2, the first of a non-discriminating synthetase, was solved. It differs from that of AspRS-1 but has resemblance to that of discriminating and archaeal AspRS from Pyrococcus kodakaraensis. The protein presents non-conventional features in its OB-fold anticodon-binding domain, namely the absence of a helix inserted between two beta-strands of this fold and a peculiar L1 loop differing from the large loops known to interact with tRNA(Asp) identity determinant C36 in conventional AspRSs. In AspRS-2, this loop is small and structurally homologous to that in AsnRSs, including conservation of a proline. In discriminating Pyrococcus AspRS, the L1 loop, although small, lacks this proline and is not superimposable with that of AspRS-2 or AsnRS. Its particular status is demonstrated by a loop-exchange experiment that renders the Pyrococcus AspRS non-discriminating. PubMed: 12660169DOI: 10.1093/emboj/cdg148 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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