EC Number   |
Reference |
|---|
   4.2.99.21 | apo-structure, to 2.35 A resolution, has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure, to 1.95 A resolution, has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis |
708989 |
| 4.2.99.21 | crystal structure of Irp9 and of its complex with the reaction products salicylate and pyruvate at 1.85 A and 2.1 A resolution, respectively. Irp9 has a complex alpha/beta fold. The crystal structure of Irp9 contains one molecule each of phosphate and acetate derived from the crystallization buffer. The enzyme is still catalytically active in the crystal. Both structures contain Mg2+ in the active site. There is no evidence of an allosteric tryptophan binding site |
709514 |
| 4.2.99.21 | docking studies of inhibitors (E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid, and 3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid |
708123 |
| 4.2.99.21 | molecular dynamics simulations and averaged intermolecular substrate-protein distances, active-site volumes for reactants and transition state |
708873 |
| 4.2.99.21 | native protein and selenomethionine-derivative, to 2.5-3.2 A resolution |
707474 |
| 4.2.99.21 | purified recombinant His-tagged wild-type enzyme and mutant K42E in complex with salicylate and pyruvate, hanging drop vapor diffusion method, mixing of 0.001 ml of 64 mg/ml wild-type protein with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate, 0.1 M sodium acetate, pH 4.5, and 6% glycerol, mixing of 0.001 ml of 34 mg/ml mutant protein with 0.001 ml reservoir solution containing 0.004 M Gly-Gly, 0.100 M sodium acetate, pH 3.6, and 12% glycerol, ligands in 20fold molar excess, 25°C, 24-48 h, X-ray diffraction structure determination and analysis, modeling |
714268 |
| 4.2.99.21 | to 2.5 A resolution, space group P21 |
706996 |
| 4.2.99.21 | wild-type and mutant K42E, to 1.95 and 1.79 A resolution, respectively, in complex with salicylate and pyruvate |
714268 |
| 4.2.99.21 | X-ray crystallographic structures for mutant K42A with salicylate and pyruvate bound, to 2.5 A resolution, and for apo-I87T, to 2.15 A resolution. Circular dichroism studies of mutants K42A, K42Q, K42E, and K42H, A43P and I87T |
707496 |
