EC Number   |
|---|
   2.7.7.52 | apoenzyme and enzyme in complex with UTP or ATP, hanging drop vapor diffusion method, using 13-15% (w/v) PEG3350 as the precipitant |
| 2.7.7.52 | enzyme bound to uridine-5'-[(alpha,beta)-imido]triphosphate, hanging drop vapor diffusion method, using 20% (v/v) glycerol ethoxylate. Enzyme bound to GpU, sitting drop vapor diffusion method, using 30% (v/v) glycerol ethoxylate and 60 mM sodium malonate, pH 7.0. Enzyme bound to CACAGU, hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 75 mM sodium malonate, pH 7.0. Enzyme bound to U6 RNA, sitting drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 90 mM sodium malonate, pH 7.0 |
| 2.7.7.52 | enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350 |
| 2.7.7.52 | Lin28-interacting module of TUT4, sitting drop vapor diffusion method, using 100 mM HEPES-NaOH, pH 7.0, 20% (w/v) PEG3350, 3% (v/v) 2-methyl-2,4-pentanediol, 200mM ammonium citrate, and 3% (w/v) 1,5 diaminopentane dihydrochloride |
| 2.7.7.52 | mutant enzyme D547A, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 6000 and 5% (w/v) 2-methyl-2,4-pentanediol |
| 2.7.7.52 | purified recombinant N-terminally His-tagged TUT4, free or with bound 2'-deoxyribonucleoside, at a concentration of 10 mg/mL in 10 mM HEPES, pH 7.6, 70 mM KCl, 0.5 mM DTT, and in presence of 4 mM MgCl2 and 0.05 mM UTP, screening with commercial crystallization screens, vapor diffusion technique, 4°C, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution |
| 2.7.7.52 | small plate-like co-crystals of purified recombinant N-terminally His-tagged TbTUT4 and UTP grow in 100 mM sodium cacodylate (pH 6.5), 200 mM calcium acetate, 18% (w/v) PEG-8000, crystal structure reveals two significantly different conformations of this TUTase:one molecule is in a relatively open apo confirmation, whereas the other displays a more compact TUTase-UTP complex |
| 2.7.7.52 | structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate. |
| 2.7.7.52 | TUT4 in complex with UTP, X-ray diffraction structure analysis |
