1D2D
Hamster EprS second repeated element. NMR, 5 structures
Summary for 1D2D
| Entry DOI | 10.2210/pdb1d2d/pdb |
| Related | 1R1B |
| Descriptor | TRNA SYNTHETASE (1 entity in total) |
| Functional Keywords | trna synthetase (ligase), protein transcription, ligase |
| Biological source | Cricetulus griseus (Chinese hamster) |
| Total number of polymer chains | 1 |
| Total formula weight | 6721.82 |
| Authors | Cahuzac, B.,Berthonneau, E.,Birlirakis, N.,Guittet, E.,Mirande, M. (deposition date: 1999-09-23, release date: 2000-05-24, Last modification date: 2024-05-22) |
| Primary citation | Cahuzac, B.,Berthonneau, E.,Birlirakis, N.,Guittet, E.,Mirande, M. A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J., 19:445-452, 2000 Cited by PubMed Abstract: Aminoacyl-tRNA synthetases of higher eukaryotes possess polypeptide extensions in contrast to their prokaryotic counterparts. These extra domains of poorly understood function are believed to be involved in protein-protein or protein-RNA interactions. Here we showed by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl-prolyl-tRNA synthetase had a general RNA-binding capacity. The solution structure of one of these repeated motifs was also solved by NMR spectroscopy. One repeat is built around an antiparallel coiled-coil. Strikingly, the conserved lysine and arginine residues form a basic patch on one side of the structure, presenting a suitable docking surface for nucleic acids. Therefore, this repeated motif may represent a novel type of general RNA-binding domain appended to eukaryotic aminoacyl-tRNA synthetases to serve as a cis-acting tRNA-binding cofactor. PubMed: 10654942DOI: 10.1093/emboj/19.3.445 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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