EC Number |
---|
6.5.1.4 | - |
6.5.1.4 | crystal structure of the enzyme in complex with a 3'-phosphate terminated RNA and adenosine in the AMP-binding pocket |
6.5.1.4 | crystallized in the states St-Rtc, St-Rtc+Mn, St-Rtc+ATP, St-Rtc+AMP and St-Rtc-AMP |
6.5.1.4 | hanging drop vapor diffusion technique, 2 orthorhombic crystal forms, space group P2(1)2(1)2(1), unit-cell dimensions a : 101.8 A, b : 126.6 A and c : 128.8 A, and P2(1)2(1)2 with unit cell dimensions a : 125.8 A, b : 133.5 A, c : 51.0 A |
6.5.1.4 | native enzyme, with AMP covalently bound, in complex with AMP, with ATP, or Mn2+, at 2.25 A, 2.25A, 2.9 A, 2.4 A and 3.2 A resolutions, respectively. Upon binding of Mg2+ to residue E10, the triphosphate group of the trapped ATP changes its conformation, with help of ligands R17 and R39. The Nepsilon atom of H307 attacks the alpha-phosphate group to form a new P-N bond. When a truncated RNA is bound, its 3'-phosphate group may be forced to react with the phosphate group of AMP, and the activiated 3'-phosphate group may be attacked by the 2'-hydroxyl group to generate the 2',3'-cyclic phosphodiester |