EC Number   |
|---|
   3.2.1.142 | in complex with its endogenous inhibitor LDI, at 2.7 A resolution. A hydrophobic cluster flanked by ionic interactions in the protein-protein interface is vital for the picomolar affinity of LDI to the enzyme |
| 3.2.1.142 | in complex with the competitive inhibitor beta-cyclodextrin, hanging drop vapor diffusion method, with streak seeding in a reservoir solution of 22% (w/v) PEG 3350, 5% (v/v) Gol, and 0.3 M NaI, or without seeding in a reservoir solution of 30% (w/v) PEG 3350, 10% (v/v) Gol, and 0.3 M NaI. In complex with the competitive inhibitor alpha-cyclodextrin, hanging drop vapor diffusion method, without seeding in a reservoir solution of 30% (w/v) PEG 3350 and 0.3 M NaI |
| 3.2.1.142 | purified free enzyme with a glycerol molecule in the active site or purified enzyme in complex with competitive inhibitors alpha- and beta-cyclodextrin, hanging drop vapour diffusion method, streak-seeding, mixing of 10 mg/mlprotein in 50 mM MES buffer pH 6.6, 250 mM NaCl, 0.5 mM CaCl2, 0.67mM maltotriose, with a reservoir solution consisting of 30% w/v PEG 3350, 5% glycerol, 0.3 M NaI, cysteine is added to the crystallization drops to a final concentration of 5-7 mM, one week, 20°C, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular replacement and modelling |
| 3.2.1.142 | structures of barley limit dextrinase and active-site mutants in complex with natural substrates, products and substrate analogues. Avoidance of alpha-1,4-hydrolytic activity and strong preference for alpha-1,6-hydrolytic activity seems to be based on the strong interaction to Trp512 and Phe553 on each flank of the catalytic cleft, which will keep non-branched polysaccharides out of the reach of the catalytic nucleophile and acid-base catalyst |
