EC Number   |
Reference |
|---|
    2.7.7.12 | 17.5-23 mg/ml recombinant protein, hanging drop vapour diffusion method in the presence of 4 mM substrate analog phenyl-UDP, 277 K, 0.1 M sodium succinate, pH 5.9, 0.25 M NaCl, 0.4 M Li2SO4, over 14.5% w/w polyethylene glycol 10000, 1 mM NaN3, 5-6 days, X-ray diffraction structure determination and analysis |
642825 |
| 2.7.7.12 | crystal structure determination and analysis |
722427 |
| 2.7.7.12 | crystal structure of ternary complex reveals a homodimer arrangement that contains a covalent uridylylated intermediate and glucose 1-phosphate in the active site, as well as a structural zinc-binding site, per monomer. Both uridylylation and zinc binding influence the stability and aggregation tendency of human GALT. Q188R, the most commonly detected disease-associated variant, increases the rate of aggregation in the absence of zinc likely due to its reduced ability to form the uridylylated intermediate |
738352 |
| 2.7.7.12 | H166G mutant enzyme/UDP-glucose or UDP-galactose complexes, X-ray diffraction structure determination and analysis |
642848 |
| 2.7.7.12 | purified recombinant enzyme, sitting-drop vapour-diffusion method, 10mg/ml protein, 4°C, X-ray diffraction structure determination and analysis at 2.73 A resolution |
721231 |
| 2.7.7.12 | sitting-drop vapor diffusion method, two different crystal structures of Pyrobaculum aerophilum galactose 1-phosphate uridylyltransferase (GalT) are determined: the substrate-free enzyme at 2.33 A and the UDP-bound H140F mutant enzyme at 1.78 A |
762352 |
| 2.7.7.12 | sitting-drop vapour diffusion at 20°C. 1.9 A resolution crystal structure of human GALT ternary complex reveals a homodimer arrangement that contains a covalent uridylylated intermediate and glucose-1-phosphate in the active site, as well as a structural zinc-binding site, per monomer |
761227 |
| 2.7.7.12 | uridyl/enzyme complex, X-ray diffraction structure determination and analysis |
642848 |
