EC Number   |
|---|
   6.2.1.54 | crystal structure of a DltA is determined at 2.0 A resolution in complex with the D-alanine adenylate intermediate of the first reaction. Despite the low level of sequence similarity, the DltA structure resembles known structures of adenylation domains such as the acetyl-CoA synthetase. The enantiomer selection appears to be enhanced by the medium-sized side chain of Cys-269 |
| 6.2.1.54 | hanging drop vapor diffusion method, using 0.1 M MgCl2, 0.5 M KCl, 16% (w/v) polyethylene glycol 3350 and 0.05 M HEPES-NaOH buffer at pH 7.2 |
| 6.2.1.54 | protein is crystallized in the presence of substrates D-Ala, ATP and MgCl2. The structures of the reported DltA reveal the determinants for D-Ala substrate specificity, and confirm that the PCP-activating domains are able to adopt multiple conformational states, in this case corresponding to the thiolation reaction |
| 6.2.1.54 | substrate-free form, to 1.9 A resolution, space group P21 |
| 6.2.1.54 | the crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) is determined in complex with ATP to 1.9 A resolution |
