EC Number   |
|---|
    2.5.1.31 | - |
| 2.5.1.31 | apoenzyme and enzyme bound to dimethylallyl diphosphate, geranyl diphosphate and dimethylallyl diphosphate plus S-thiologeranyl diphosphate |
| 2.5.1.31 | C234A UPPS mutant to prevent intra-molecular disulfide bond formed during the long period of crystallization process is crystallized using the hanging drop method. The protein is a dimer and each subunit contains a catalytic domain and a pairing domain. Two subunits are tightly associated through the central beta-sheet and a pair of long alpha-helices. Helicobacter pylori UPPS has a 1.5-turn shorter alpha5 helix in the dimer interface. This may weaken the dimer formation for Helicobacter pylori UPPS. The catalytic domain is composed of six beta-strands and four beta-helices and the central tunnel-shaped active site is surrounded by 2 alpha-helices and 4 beta-strands |
| 2.5.1.31 | co-crystal structure of UPPS in complex with (2E,6E)-farnesyl diphosphate |
| 2.5.1.31 | crystal structure of Helicobacter pylori UPPS and mutant by hanging drop method |
| 2.5.1.31 | hanging drop set-up |
| 2.5.1.31 | hanging-drop method |
| 2.5.1.31 | in complex with farnesyl diphosphate. Virtual screening of inhibitors from a library of 58,635 compounds, modelling of inhibitors N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamide and 3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamide into structure |
| 2.5.1.31 | purified His-tagged wild-type enzyme in complex with Mg2+, sulfates, and 2 molecules of Triton X-100, hanging drop vapour diffusion method, 0.002 ml protein solution containing 10 mg/ml protein, 2% Triton X-100, 5 mM MgCl2, and 0.66 mM farnesyl diphosphate, is mixed with equal volume of mother liquid containing 0.01 M CoCl2, 0.1 M MES, pH 6.5, and 1.8 M ammonium sulfate, equilibration against 0.2 ml mother liquid at 25°C, 10 days, X-ray diffraction structure determination and analysis at 1.73 A resolution, modeling |
| 2.5.1.31 | purified His-tagged wild-type enzyme, hanging drop vapour diffusion method, high concentration of sulfate or phosphate in the mother liquid to prevent binding of Triton X-100 or substrates during crystallization, 0.002 ml mother liquid containing 25% ethylene glycol, pH 7.5, mixed with 0.002 ml protein solution containing 10 mg/ml protein, 1 mM peptide, 0.05% Triton X-100, and 0.5 mM MgCl2, equilibration against 0.2 ml mother liquid at 25°C, 5 days, crystals are then soaked in mother liquid containing 0.23 mM farnesyl diphosphate, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling |
