EC Number |
Reference |
---|
3.5.2.17 | - |
644455 |
3.5.2.17 | at 4°C by the sitting-drop, vapour diffusion method, using 0.1 M HEPES (pH 7.5), 20% (w/v) PEG 10000 |
688335 |
3.5.2.17 | hanging drop vapour diffusion method in 0.1 M sodium cacodylate (pH 6.0), 0.2 M MgCl2, 20% (w/v) polyethylene glycol 3350 at 22°C |
688334 |
3.5.2.17 | mutants Y116T, I16A/Y116T and mutant I16A/Y116T in complex with thyroxine, to 1.7 A, 2.3 A., and 1.95 A resoultion. Structural comparison of HIUase and transthyretin, TTR. Mutations Y116T and I16A are likely to be crucial events in order to induce, after a gene duplication event, the conversion of the enzyme HIUase into a binding protein, transthyretin. The mutations at the active sites of HIUase open up the two ends of the channel that transverses the entire tetrameric protein, generating two cavities accessible to the thyroxine molecule and abrogating, at the same time, the enzymatic activity |
720251 |
3.5.2.17 | to 1.8 A resolution, and modeling of substrate 5-hydroxyisourate into the active site. The four chains of the enzyme come together to form a homotetramer with 222 symmetry. The tetramer is a dimer of dimers, with two protomers arranged to create an extended beta-sheet that makes up the dimerdimer interface |
718476 |