EC Number   |
|---|
  1.1.1.305 | crystal structure analysis, PDB entry 1Z7E |
| 1.1.1.305 | crystal structure of the ArnA decarboxylase domain |
| 1.1.1.305 | crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90° |
| 1.1.1.305 | hanging drop vapor diffusion method, crystal structure of the full-length bifunctional ArnA with UDP-glucuronic acid and ATP bound to the dehydrogenase domain. Binding of UDP-glucuronic acid triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-glucuronic acid |
| 1.1.1.305 | purified recombinant UXS85-420 lacking the N-terminal membrane-spanning domain, hanging drop vapor diffusion method, precipitant containing 1.3 M ammonium sulfate, 0.1 M magnesium formate, and 0.15% PEG at 26°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement |
| 1.1.1.305 | structure of apo-ArnA and comparison with its ATP- and UDP-glucuronic acid-bound counterparts. In the crystal structure, a binding pocket at the centre of each ArnA trimer in its apo state pocket is occupied by a dithiothreitol molecule. Formation of the pocket is linked to a cascade of structural rearrangements that emerge from the NAD+-binding site. A small effector molecule is postulated that binds to the central pocket and modulates the catalytic properties of ArnA |
