EC Number   |
|---|
    3.6.1.1 | - |
| 3.6.1.1 | at 2.7 A resolution. Comparison with Thermus thermophilus and Escherichia coli enzymes |
| 3.6.1.1 | CD and FTIR spectra demonstrate a similar overall fold for enzyme and PPases from Escherichia coli and Thermus thermophilus |
| 3.6.1.1 | complexed enzyme with each enzyme monomer containing the diphosphate analogue imidodiphosphate and three metal ions per active site: two Mn2+ ions in sites M1 and M2 and an Mg2+ ion in site M3, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement |
| 3.6.1.1 | different forms depending on the presence of NH4Cl or (NH4)2SO4 (alpha3'alpha3'') |
| 3.6.1.1 | isoform PpaC in complex with Mn2+, hanging drop vapor diffusion method, using 1.32 M ammonium citrate tribasic |
| 3.6.1.1 | purified enzyme bound to catalytic metals, to substrate diphosphate, and to one or two inorganic phosphate ions, hanging drop vapour diffusion method, mixing of 0.001 ml of 14 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 1.65 M NaKHPO4, 100 mM HEPES, pH 7.75, and 2 mM CaCl2, xthe crystals of Mtb PPiase in complex with two phosphate ions are obtained with the reservoir solution composed of 1.6 M KH2PO4, 100 mM HEPES, pH 7.75, and 2 mM CaCl2, and the crystals of Mtb PPiase in complex with one phosphate are obtained with the reservoir solution containing 1.57 M NaKHPO4, 100 mM HEPES pH 7.75 and 2 mM MnCl2, 22°C, X-ray diffraction structure determination and analysis at 1.85-3.30 A resolution, molecular replacement with the structure of the Mtb PPiase-Mg2+ complex as a search model |
| 3.6.1.1 | purified enzyme, vapour diffusion method, mixing of 10 mg/ml protein solution with 10% PEG 4000, 20% glycerol, 0.03 M glycols, and 0.1 M HEPES/MOPS, pH 7.5, 20°C, 6-8 days, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement method using ScPPase (PDB ID 1WGJ) as a template |
| 3.6.1.1 | purified enzyme, X-ray diffraction structure determination and analysis |
| 3.6.1.1 | purified recombinant detagged enzyme in complex with inhibitor 2,4-bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine or N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine, hanging drop vapour diffusion method, mixing of 7 mg/ml protein in 40 mM Tris-HCl pH 8.0, 100 mM NaCl, and 2 mM 2-mercaptoethanol, with reservoir solution containing 0.1 M HEPES pH 7.5, 1.6 M NaH2PO4, and 0.2 M KH2PO4, or 0.1 M HEPES pH 7.75, 1.4 M KH2PO4, and 2 mM CaCl2, respectively, 22°C, overnight, X-ray diffraction structure determination and analysis at 2.65 A and 2.45 A resolution, respectively. 2,4-Bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine is co-crystallized, while N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine is bound by soaking |
