EC Number   |
|---|
   1.14.11.55 | apo-enzyme crystallizes in space group C2221, the iron-supplemented form displays a P212121 symmetry. The apo form contains one monomer per asymmetric unit whereas the Fe-supplemented form contains a dimer |
| 1.14.11.55 | crystal structure in complex with Fe3+ at a resolution of 1.85 A. The core of the EctD structure consists of a double-stranded beta-helix forming the main portion of the active-site of the enzyme. The positioning of the iron ligand in the active site is mediated by an evolutionarily conserved 2-His-1-carboxylate iron-binding motif. The side chains of the three residues forming this iron-binding site protrude into a deep cavity in the EctD structure that also harbours the 2-oxoglutarate cosubstrate-binding site |
| 1.14.11.55 | crystal structure in its apo-form, in complex with iron, and in complex with iron, cosubstrate 2-oxoglutarate, and 5-hydroxyectoine. The iron and 2-oxoglutarate ligands are bound within the active site in a fashion similar to that found in other members of the dioxygenase superfamily. 5-Hydroxyectoine is bound by residues residues His144, His245, and Asp146 forming the 2-His-1-carboxylate facial triad |
| 1.14.11.55 | modeling and docking of different substrates into the crystal structure. The spatial positioning of homoectoine and its hydroxylated derivative in the reaction chamber are super-imposable with that of the 5-hydroxyectoine molecule |
| 1.14.11.55 | structural comparison, molecular dynamics simulations, and site-directed mutagenesis suggest the positioning of the iron, ectoine, and 2-oxoglutarate ligands in close proximity to each other and with a spatial orientation that will allow the region-selective and stereo-specific hydroxylation of (4S)-ectoine to (4S,5S)-5-hydroxyectoine |
| 1.14.11.55 | to 1.9 A resolution, and comparison of iron-bound and apo structure. The iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/EĀ
H motif, the so-called 2-His-1-carboxylate facial triad |
| 1.14.11.55 | to 2.4 A resolution, space group P1, with unit-cell parameters a 45.18 A, b 58.87 A, c 68.81 A, alpha 77.48 degrees, beta 86.03 degrees, gamma 66.97 degrees. The asymmetric unit contains two molecules with a Mattews coefficient of about 2.44 A3/Da and a solvent content of 49.53% |
