EC Number   |
Reference |
|---|
  5.4.99.23 | 2.0 A structure of the catalytic domain of RluD (residues 77326). The catalytic domain folds into a mainly antiparallel beta-sheet flanked by several loops and helices. A positively charged cleft that presumably binds RNA leads to the conserved Asp139. The RluD N-terminal S4 domain, connected by a flexible linker, is disordered in our structure. RluD is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RsuA, TruB, and TruA |
706712 |
| 5.4.99.23 | crystallization of selenomethionine-substituted RluD by the hanging-drop method, crystals diffract to 1.9 A and belong to space group P4(3)2(1)2, with unit cell parameters a = b = 75.14, c = 181.81 A |
649216 |
| 5.4.99.23 | crystals of full-length RluD are grown at 20°C using the hanging drop method. The S4 domain of RluD appears to be highly flexible or unfolded and is completely invisible in the electron density map |
702207 |
| 5.4.99.23 | crystals of SeMet-labeled DELTARluD are obtained under oil by the microbatch method, crystal structure of the catalytic module of RluD (residues 68326, DELTARluD) refined at 1.8 A to a final R-factor of 21.8%. DELTARluD is a monomeric enzyme having an overall mixed alpha/beta fold. The DELTARluD molecule consists of two subdomains, a catalytic subdomain and C-terminal subdomain with the RNA-binding cleft formed by loops extending from the catalytic sub-domain. Comparison of the structure with other pseudouridine synthases |
652934 |
