EC Number   |
Reference |
|---|
    5.1.1.7 | by using the sitting-drop vapour-diffusion method with droplets consisting of 150 nl protein solution and 150 nl reservoir solution, conditions that yield crystals are replicated using the hanging-drop vapourdiffusion method with drops containing 0.002 ml protein solution and 0.002 ml precipitant solution, crystals are obtained in space group P41212 and diffract to 2.0 A resolution, with unit-cell parameters a = b = 89.4, c = 179.6 A |
701554 |
| 5.1.1.7 | co-crystals of the inhibitors LL- and DL-aziridino diaminopimelic acid with diaminopimelate epimerase from Haemophilus influenzae are grown at room temperature by the hanging-drop vapor-diffusion method. Crystals of both complexes are obtained in 2.8 M sodium acetate /0.1 M Hepes (pH 7.0) at a protein concentration of approx. 10 mg/ml in 25 mM Hepes, 5 mM DTT (pH 8.0) |
676873 |
| 5.1.1.7 | comparisons of the mutant structures with the structures of the AziDAP inhibitor-bound form reveal that the enzyme adopts an open conformation in the absence of substrates or inhibitors with the two active site cysteines existing as a thiolthiolate pair. Substrate binding to the C-terminal domain triggers the closure of the N-terminal domain coupled with tight encapsulation of the ligand, stabilization of the conformation of an active site loop containing Cys73 and expulsion of water molecules with concomitant desolvation of the thiolate base |
671810 |
| 5.1.1.7 | crystal structure of the ligand-free form refines to a resolution of 2.6 A, 2.5 mM dithiothreitol is present in the crystal drop |
701470 |
| 5.1.1.7 | crystal structures of diaminopimelate epimerase from Haemophilus influenzae with two different isomers of the irreversible inhibitor and substrate mimic aziridino diaminopimelic acid at 1.35- and 1.70-A resolution are analysed. These structures permit a detailed description of this pyridoxal 5-phosphate-independent amino acid racemase active site and delineate the electrostatic interactions that control the exquisite substrate selectivity of DAP epimerase. Moreover, the active site shows how deprotonation of the substratesnonacidic hydrogen at the alpha-carbon by a seemingly weakly basic cysteine residue is facilitated by interactions with two buried alpha-helices |
676873 |
| 5.1.1.7 | crystallization of C73S and C217S mutant diaminopimelate epimerase enzymes of Haemophilus influenzae are obtained by the hanging-drop vapor diffusion method and submitted to X-ray structure analysis |
671810 |
| 5.1.1.7 | hanging-drop vapour-diffusion method, space group C222(1), unit cell parameters a = 98.64 A, b = 113.87 A, c = 64.48 A, 1.75 A resolution |
660601 |
| 5.1.1.7 | in complex with two different isomers of inhibitor 2-(4-amino-4-carboxybutyl)-aziridine-2-carboxylate, at 1.95 and 2.3 A resolution. Ligand binding to a cleft between the two domains of the enzyme is accompanied by domain closure with strictly conserved cysteine residues, Cys99 and Cys254, positioned to perform acid/base catalysis via a carbanion stabilization mechanism on the stereogenic alpha-carbon atom of the amino acid. Stereochemical control in catalysis is achieved by means of a highly symmetric catalytic site that can accommodate both the L and D stereogenic centers of DAP at the proximal site, whereas specific interactions at the distal site require only the L configuration |
693680 |
| 5.1.1.7 | purified enzyme CgDapF in both oxidized and reduced forms, selenium-substituted crystal, hanging drop vapor diffusion method, mixing of 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.0, for the oxidized enzyme form and 1.4 M sodium phosphate monobasic/0.9 M potassium phosphate dibasic, 0.1 M CAPS, pH 10.0, 0.2 M lithium sulfate, and 1 mM 1,4-DTT for the reduced enzyme form, the crystals of CgDapF in complex with DL-DAP are crystallized in the condition of 1.3 M sodium citrate, 0.1 M CHES, pH 9.0, and 10 mM DAP isomer, equilibration against 0.5 ml, 20°C, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution, single-wavelength anomalous dispersion method, molecular replacement |
749346 |
| 5.1.1.7 | purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 14 mg/ml protein in 20 mM HEPES, pH 7.0, 100 mM NaCl, and 5 mM DTT, with 0.001 ml of reservoir solution containing 2 M ammonium sulfate, 0.1 M sodium HEPES, pH 7.5, and 4.9-5.1% PEG 400, equilibration against reservoir solution, 25% v/v PEG 400 as a cryoprotectant, method optimization, X-ray diffraction structure determination and analysis at 1.9 A resolution |
726632 |
