EC Number   |
|---|
    3.1.2.2 | determined at 1.05 A, revealing a hotdog hydrolase fold arranged as a dimer of dimers. A second crystal structure at 1.40 A iss obtained from a crystal that is grown in the presence of Mg2+, which reveals the presence of a binding site for divalent cations at a crystal contact. The Mg2+-bound structure shows localized conformational changes, and its active site is unoccupied, suggesting a mechanism to open the active site for substrate entry or product release |
| 3.1.2.2 | docking studies to the pocket of the catalytic triad Ser 2308, His 2481, and Asp 2338, using palmitate, and fatty acids with chain lengths of 12 to 20 carbon atoms. The ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity. Binding of palmitate results in the most favorable binding free enrgy among the fatty acids tested. The experimentally amino acids of the catalytic triad Ser2308, His2481, and Asp2338 are located very close to the carboxyl group of palmitate. The close location of Arg2482 to the carboxyl group of palmitate and the catalytic triad implies an important role of this residue in catalysis |
| 3.1.2.2 | hanging drop method, protein solution: 10 mg/ml, 5 mM NH4OH, 2 mM DTT, over equal volume of reservoir solution: 1-2 M NaCl, 0.1 M sodium formate, pH 6.0, 2 mM N,N-dimethyl-dodecylamine oxide-LDAO, few days, X-ray structure determination and analysis |
| 3.1.2.2 | hanging-drop vapor diffusion in 20% PEG 2000. Crystal structures of both the N- and C-terminal domains of the mouse enzyme. The quaternary arrangement in Acot7 features a trimer of hotdog fold dimers |
| 3.1.2.2 | hanging-drop vapor-diffusion method, crystal structure to 2.3 A resolution. FcoT crystals, produced in the presence of the substrate dodecenoyl-CoA, are cubic and belong to space group I2(1)3, with one molecule in the asymmetric unit |
| 3.1.2.2 | purified recombinant His-tagged enzyme, 76.8 mg/ml, hanging-drop vapour-diffusion method, protein solution: 10 mM sodium phosphate, pH 7.0, plus equal volme of reservoir solution: 0.2 M ammonium sulfate, 27% w/w PEG-MME 5K, 0.1 M 2-[N-morpholino]ethanesulfonic acid, pH 6.5, room temperature, crystals appeared after 7-21 d, X-ray diffraction structure determination and analysis at 2.4 A resolution |
| 3.1.2.2 | vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 17°C. Crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 A, gamma = 120°). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4 A resolution using the laboratory X-ray source and are suitable for crystal structure determination |
| 3.1.2.2 | vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 17°C. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 A, gamma = 120°). Two molecules in the asymmetric unit. The crystals diffract to 2.4 A resolution |
