1YI8
Crystal structure of tryptophanyl trRNA synthetase II from Deinococcus radiodurans in complex with L-Trp
Summary for 1YI8
| Entry DOI | 10.2210/pdb1yi8/pdb |
| Descriptor | tryptophanyl-tRNA synthetase, TRYPTOPHAN (3 entities in total) |
| Functional Keywords | auxiliary tryptophanyl trna synthetase, ligase |
| Biological source | Deinococcus radiodurans |
| Total number of polymer chains | 3 |
| Total formula weight | 114880.98 |
| Authors | Buddha, M.R.,Crane, B.R. (deposition date: 2005-01-11, release date: 2005-02-22, Last modification date: 2024-02-14) |
| Primary citation | Buddha, M.R.,Crane, B.R. Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat.Struct.Mol.Biol., 12:274-275, 2005 Cited by PubMed Abstract: The most divergent of two tryptophanyl tRNA synthetases (TrpRS II) found in Deinococcus radiodurans interacts with a nitric oxide synthase protein that produces 4-nitro-tryptophan (4-NRP). TrpRS II efficiently charges transfer RNA(Trp) with 4-NRP and 5-hydroxy-tryptophan (5-HRP). The crystal structures of TrpRS II bound to tryptophan and 5-HRP reveal residue substitutions that accommodate modified indoles. A class of auxiliary bacterial TrpRSs conserve this capacity to charge tRNA with nonstandard amino acids. PubMed: 15723076DOI: 10.1038/nsmb907 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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