EC Number   |
|---|
    6.1.1.6 | - |
| 6.1.1.6 | (alpha2)2 LysRS tetramer |
| 6.1.1.6 | crystal structure of lysyl-tRNA synthetase complexed with Escherichia coli tRNALys |
| 6.1.1.6 | crystal structures of two complexes of LysRS with the adenylate of L-lysine hydroxamate and with 5'-O-[N-(L-Lysyl)sulphamoyl] adenosine. The comparisons of the two structures and the SerRS structure reveals the specific side-chain shift of Glu411 of LysRS in the complex with the adenylate of L-lysine hydroxamate. Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack |
| 6.1.1.6 | determined to 2.8 A resolution with lysine bound to the active site |
| 6.1.1.6 | hanging drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 2% (v/v) tascimate pH 6.0, 20% (w/v) PEG 3350 |
| 6.1.1.6 | in complex with p38/AIMP2 |
| 6.1.1.6 | micrositting drop-vapor diffusion method, both DELTAS70-T584 and full length LysRS |
| 6.1.1.6 | purified enzyme free or in complex with ATP, Lys-AMP, or AMPPNP, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution, the latter contains: for the free enzyme KRS 100 mM HEPES pH 7.5, 10% PEG 6000, and 5% 2-methyl-2,4-pentanediol, for the KRS-Lys-AMP crystals 50 mM HEPES, pH 8.0, 50 mM NaCl, 1 mM spermine, and 8% PEG 4000, for the KRS-ATP crystals 50 mM HEPES pH 8.0, 50 mM NaCl, 7.5% PEG 4000,and 1.2 mM spermine, and for the KRS-AMPPNP crystals 50 mM HEPES pH 8.0, 50 mM NaCl, 7.5% PEG 4000, and 1.2 mM spermine, 3 days, 20°C, X-ray diffraction structure determination and analysis at 2.80-3.05 A resolution, molecular replacement using HsKRS structure, PDB ID 3BJU, as the search model, modeling |
| 6.1.1.6 | purified enzyme PfKRS in complex with lysine and cladosporin, hanging drop vapour diffusion method, mixing of 0.001 ml of highly pure enzyme in 50 mM Tris-HCl, pH 8.0, 200 mM NaCl, 10 mM 2-mercaptoethanol, 0.5 mM cladosporin, and 2 mM L-lysine, with 0.001 ml of crstallization solution containing 0.1 M Bis-Tris, pH 6.5, 2% v/v Tascimate, pH 6.0, 20% w/v PEG 3350, 20°C, 10 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular homology modeling using the human enzyme structure as template |
