EC Number   |
|---|
    3.1.8.1 | - |
| 3.1.8.1 | crystal structure analysis of SsoPox in the apo form and in complex with a quorum-sensing lactone mimic at 2.6 and 2.0A resolution, respectively, overview |
| 3.1.8.1 | hanging drop vapour diffusion method |
| 3.1.8.1 | hanging drop vapour diffusion method, in 10% PEG6000, 0.1 M HEPES, pH 7.0, 1% diethyl 4-methylbenzylphosphonate, and 5 mM sodium azide |
| 3.1.8.1 | in complex with diisopropyl methyl phosphonate and with triethyl phosphate |
| 3.1.8.1 | in the presence of Co2+, by vapor diffusion method in hanging drop, to 2.36 A resolution. The active site contains three substrate binding pockets: the small (F28, Y30, T70, C74, V268, and W271), large (R230, I233, M236, V237, and W289) and leaving group (Y100 and E103) pockets. Metal binding site contains a tyrosine residue at position 97 in close proximity to the beta-metal |
| 3.1.8.1 | phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6 |
| 3.1.8.1 | protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another |
| 3.1.8.1 | purified recombinant enzyme complexed with Co2+, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 6.4 mg/ml protein in 50 mM Hepes, pH 7.0, 150 mM NaCl, and 1 mM CoCl2, are mixed with 0.005 ml of reservoir solution that consists of 20% w/v PEG 3350 and 0.2 M sodium nitrate, X-ray diffraction structure determination and analysis at 1.9 A resolution |
| 3.1.8.1 | purified recombinant enzyme mutant G137D, hanging drop vapor diffusion method, the reservoir solution contains 100 mM sodium-acetate, pH 4.6, and 20% PEG 2000 monomethyl ester, 17°C, X-ray diffraction structure determination and analysis at 2.01 A resolution, molecular replacement using the previously determined structure of LcalphaE7, PDB ID 4FNG, as template, model building |
