EC Number   |
Reference |
|---|
  2.1.1.190 | crystal structures of apo-form RlmCD and its complex with SAH. A long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity |
758157 |
| 2.1.1.190 | hanging drop vapor diffusion method, the crystal structure is determined at 1.95 A resolution using a single crystal of the selenomethionyl protein. The protein is organized into three structural domains. The N-terminal domain (residues 1574) is the smallest domain and is composed of five beta strands. The central domain (residues 7592 and 125262) and the catalytic domain (residues 93124 and 263431) are juxtaposed, and a concave surface is formed at the interface between them |
706781 |
| 2.1.1.190 | hanging drop vapor diffusion method, the structure of a ternary complex containing RumA, S-adenosylhomocysteine and a covalently bound 23S rRNA fragment(19321968) with 5-fluoro-uridine at position 1939 is determined by molecular replacement methods |
703145 |
| 2.1.1.190 | structure of RlmCD in complex with its cofactor and the RNA substrate containing U747 at 2.00 A or U1939 at 3.10 A. The side-chain rearrangement of F145 displays an unusual mechanism through which RlmCD can discriminate between U747- and U1939-containing RNA substrate by switching the intermolecular aromatic stacking between protein and RNA on/off |
758197 |
