4H3S
The Structure of Glutaminyl-tRNA Synthetase from Saccharomyces Cerevisiae
Summary for 4H3S
| Entry DOI | 10.2210/pdb4h3s/pdb |
| Related | 3TL4 |
| Descriptor | Glutamine-tRNA ligase, ZINC ION, GLYCEROL, ... (8 entities in total) |
| Functional Keywords | rossmann fold, ligase, appended domain, trna synthetase, beta barrel anticodon binding domain, pseudo zinc finger motif |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 95425.80 |
| Authors | Snell, E.H.,Grant, T.D. (deposition date: 2012-09-14, release date: 2013-04-24, Last modification date: 2023-09-20) |
| Primary citation | Grant, T.D.,Luft, J.R.,Wolfley, J.R.,Snell, M.E.,Tsuruta, H.,Corretore, S.,Quartley, E.,Phizicky, E.M.,Grayhack, E.J.,Snell, E.H. The Structure of Yeast Glutaminyl-tRNA Synthetase and Modeling of Its Interaction with tRNA. J.Mol.Biol., 425:2480-2493, 2013 Cited by PubMed Abstract: Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended N-terminal domain (NTD) whose precise function is unknown. Although GlnRS structures from two prokaryotic species are known, no eukaryotic GlnRS structure has been reported. Here we present the first crystallographic structure of yeast GlnRS, finding that the structure of the C-terminal domain is highly similar to Escherichia coli GlnRS but that 214 residues, including the NTD, are crystallographically disordered. We present a model of the full-length enzyme in solution, using the structures of the C-terminal domain, and the isolated NTD, with small-angle X-ray scattering data of the full-length molecule. We proceed to model the enzyme bound to tRNA, using the crystallographic structures of GatCAB and GlnRS-tRNA complex from bacteria. We contrast the tRNA-bound model with the tRNA-free solution state and perform molecular dynamics on the full-length GlnRS-tRNA complex, which suggests that tRNA binding involves the motion of a conserved hinge in the NTD. PubMed: 23583912DOI: 10.1016/j.jmb.2013.03.043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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