EC Number   |
|---|
   3.2.2.21 | - |
| 3.2.2.21 | 2.5 A crystal structure colmplexed to DNA, crystals belong to space group P3(1)21, cell dimensions a = B = 82.4 A and c = 199.7 A |
| 3.2.2.21 | AAG complexed to DNA |
| 3.2.2.21 | AlkA in complex with undamaged DNA, sitting drop vapor diffusion method, using 25-29% (w/v) polyethylene glycol 3350, 100 mM bis-Tris, pH 6.0-6.6, 200 mM Li2S04, and 3% (w/v) 6-aminocaproic acid, at 25°C |
| 3.2.2.21 | at 1.8 A resolution. Structure contains two sodium ions in octahedral coordination |
| 3.2.2.21 | crystal structure of AlkA solved with the multiple isomorphous replacement method, crystals grown with sitting-drop vapor-diffusion technique, space group P2(1), cell dimensions a = 58.61 A, b = 76.93 A, c = 62.27 A |
| 3.2.2.21 | expression in Saccharomyces cerevisiae |
| 3.2.2.21 | hanging drop vapor difusion crystallization, space group P2(1), unit-cell parameters are a = 58.17, b = 76.27, c = 61.69, alpha = gamma = 90°, beta = 109.98° |
| 3.2.2.21 | isoform AlkA2, hanging drop vapor diffusion method, using 1 M LiCl2, 0.1 M MES pH 6.0, 10% (w/v) PEG 6000 |
| 3.2.2.21 | molecular dynamics simulations show that neutral substrates form a common DNA-protein hydrogen bond, which results in a consistent active site conformation that maximizes pi-pi interactions between the aromatic residues and the nucleobase required for catalysis. The exocyclic amino groups of the natural purines clash with active site residues, which leads to catalytically incompetent DNA-enzyme complexes due to significant reorganization of active site water. Water resides between the A nucleobase and the active site aromatic amino acids required for catalysis, while a shift in the position of the general base (E125) repositions water away from G. The methyl substituents in cationic purine lesions (3-methyladenine and 7-methyladenine) exhibit repulsion with active site residues |
