EC Number   |
|---|
    2.5.1.16 | - |
| 2.5.1.16 | construction of a crystal structure homology model, PDB ID: Q9FS5, for the Plasmodium falciparum enzyme from crystal structure 1JQ3 and 1XJ5, structure-function relationship |
| 2.5.1.16 | hanging drop vapour diffusion, multiwavelength anomalous diffraction from selenomethionine containing crystals |
| 2.5.1.16 | in apo form, in complex with S-adenosylmethioninamine in complex with and two inhibitors, S-adenosyl-1,8-diamino-3-thio-octane and trans-4-methylcyclohexylamine. Binding of S-adenosylmethioninamine stabilizes the conformation of the flexible gatekeeper loop of the enzyme and affects the conformation of the active-site amino acid residues, preparing the protein for binding of the second substrate. Inhibitor S-adenosyl-1,8-diamino-3-thio-octane essentially fills the entire active-site pocket, inhibitor trans-4-methylcyclohexylamine only occupies part of it |
| 2.5.1.16 | in complex with decarboxylated S-adenosylmethionine, trans-4-methylcyclohexylamine and inhibitors, sitting drop vapor diffusion method, using 100 mM bis-Tris pH 5.5-6.5, 200 mM ammonium sulfate, 10-15% (w/v) PEG 4000 |
| 2.5.1.16 | in complex with S-methyl-5'-thioadenosine and putrescine or inhibitors, hanging drop vapor diffusion method, using 0.1 M MES buffer pH 5.6, 0.1 M ammonium sulfate, 27% (w/v) PEG 3350 |
| 2.5.1.16 | purified recombinant enzyme free or in complex with spermidine, putrescine, 5'-methyl, 5'-deoxymethylthioadenosine, and S-adenosylmethionine, hanging drop vapor diffusion method, 20°C, 10 mg/ml protein solution is mixed with reservoir solution, containing 20-25% PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES-NaOH, pH 7.5, and ligands in a ratio of 1: 5 enzyme-ligand, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution |
| 2.5.1.16 | purified recombinant His6-tagged enzyme, also as selenomethionine-labeled enzyme, the latter from 0.1 M sodium HEPES, pH 7.5, with 33% PEG 400, two crystals Forms A and B, belonging to the monoclinic space group P21and orthorhombic space group C2221, are grown under different conditions, X-ray diffraction structure determination and analysis at 2.0-2.5 A resolution, multiwavelength anomalous dispersion |
| 2.5.1.16 | sitting drop method. Crystallographic date show in detail the structural rearrangements of the enzyme that are required to stabilize ligands within the active site |
| 2.5.1.16 | sitting drop vapor diffusion at 16°C. Crystal structure of the FliMSpeE complex is determined at 2.7 A resolution |
