EC Number   |
|---|
    6.1.1.9 | - |
| 6.1.1.9 | 1.7 A resolution crystal structure of the ValRS editing domain and 1.7 A resolution crystal structure of the editing domain bound with [N-(L-threonyl)-sulfamoyl]adenosine, hanging drop vapor diffusion method |
| 6.1.1.9 | enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis |
| 6.1.1.9 | enzyme in complex with tRNAValCAC isoacceptor and an analogue of the Val-adenylate intermediate, hanging-drop vapour diffusion method, 2 months, 4°C, 7-10 mg/ml protein/tRNA/Val-AMS solution in a molar ration of 1:1.1:2, plus equal volume of crystallization solution containing 50 mM sodium cacodylate, pH 6.5, 1.0 ammonium sulfate, 10 mM MgSO4, 6% 1,8-diaminooctane, equilibration against a reservoir solution of 50 mM sodium cacodylate, pH 6.5, 2.8 M ammonium sulfate, 10 mM MgSO4, X-ray structure determination at 2.9 A resolution and analysis |
| 6.1.1.9 | molecular dynamics simulation studies based on PDB structure ID 1wk9. Noncognate substrates Thr-AMP and Thr-A76, bind more strongly than the cognate substrates Val-AMP and Val-A76 in both pre- and post-transfer editing, respectivel |
