1JH3
Solution structure of tyrosyl-tRNA synthetase C-terminal domain.
Summary for 1JH3
| Entry DOI | 10.2210/pdb1jh3/pdb |
| Related | 2TS1 |
| NMR Information | BMRB: 5070 |
| Descriptor | TYROSYL-TRNA SYNTHETASE (1 entity in total) |
| Functional Keywords | aminoacyl-trna synthetase, anticodon-arm binding domain, ligase |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm: P00952 |
| Total number of polymer chains | 1 |
| Total formula weight | 12001.54 |
| Authors | Guijarro, J.I.,Pintar, A.,Prochnicka-Chalufour, A.,Guez, V.,Gilquin, B.,Bedouelle, H.,Delepierre, M. (deposition date: 2001-06-27, release date: 2002-03-20, Last modification date: 2024-05-29) |
| Primary citation | Guijarro, J.I.,Pintar, A.,Prochnicka-Chalufour, A.,Guez, V.,Gilquin, B.,Bedouelle, H.,Delepierre, M. Structure and Dynamics of the Anticodon Arm Binding Domain of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase Structure, 10:311-317, 2002 Cited by PubMed Abstract: The structure of a recombinant protein, TyrRS(delta4), corresponding to the anticodon arm binding domain of Bacillus stearothermophilus tyrosyl-tRNA synthetase, has been solved, and its dynamics have been studied by nuclear magnetic resonance (NMR). It is the first structure described for such a domain of a tyrosyl-tRNA synthetase. It consists of a five-stranded beta sheet, packed against two alpha helices on one side and one alpha helix on the other side. A large part of the domain is structurally similar to other functionally unrelated RNA binding proteins. The basic residues known to be essential for tRNA binding and charging are exposed to the solvent on the same face of the molecule. The structure of TyrRS(delta4), together with previous mutagenesis data, allows one to delineate the region of interaction with tRNATyr. PubMed: 12005430DOI: 10.1016/S0969-2126(02)00699-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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