EC Number |
---|
2.6.1.62 | - |
2.6.1.62 | complex of holoenzyme and 7-keto-8-aminopelargonic acid |
2.6.1.62 | crystallization of the native and the selenomethionine enzyme, without ligand in two different space groups. In both cases, the structures show a dimer made of two monomers related by a noncrystallographic twofold axis |
2.6.1.62 | hanging drop vapor diffusion method |
2.6.1.62 | in complex with inhibitors 5-(pyridin-2-yl)thiophene-2-carboxamide, 4-(1H-imidazol-1-yl)benzamide, and N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine |
2.6.1.62 | in complex with substrate 7-oxo-8-aminopelargonic acid and in complex with inhibitors 1-(1,3-benzothiazol-2-yl)methanamine and 2-hydrazinyl-1,3-benzothiazole. The side chains of Tyr25, Trp65, Arg400, and Tyr407 are shown to be quite flexible. Small molecule binding induces unexpected conformational remodeling in the substrate binding site |
2.6.1.62 | native and the selenomethionine enzyme without ligand, in two different space groups. The structures show a dimer made of two monomers related by a noncrystallographic twofold axis |
2.6.1.62 | purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 11 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.02 mM PLP, pH 7.9, with precipitant solution containing 0.1 M sodium citrate, pH 6.1, 0.2 M potassium sodium tartrate, and 1.8 M ammonium sulfate. A glass capillary containing 0.008 ml of protein solution is mounted in the gel tube with 1% agarose presoaked in 1 ml of the precipitant solution, method optimization, 1 month at 20°C. X-ray diffraction structure determination and analysis at 1.6 A resolution |
2.6.1.62 | purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20°C, 10 mg/ml protein in solution mixed with equal volume of well solution containing 26-28% PEG 4000, 9-12% methylpentanediol, 100 mM HEPES, pH 7.5, microseeding, 2 days, X-ray diffraction structure determination and analysis at 1.7-2.4 A resolution, modeling |
2.6.1.62 | to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105 |