EC Number   |
General Information |
Reference |
|---|
  2.1.1.193 | evolution |
RsmE is the founding member of a RNA methyltransferase family responsible for N3-methylation of U1498 in 16S ribosomal RNA. It is well conserved across bacteria and plants and may play an 30 important role in ribosomal intersubunit communication |
720262 |
| 2.1.1.193 | malfunction |
a yggJ deletion strain lacks the methyl group at U1498 as well as the specific methyltransferase activity. The deletion strain is unaffected in exponential growth in rich or minimal media at multiple temperatures, but it is defective when grown in competition with isogenic wild-type cells |
706714 |
| 2.1.1.193 | more |
RsmE forms a flexible dimeric conformation that is essential for substrate binding. RsmE-S-adenosyl-L-methionine-uridylic acid complex modeling and substrate binding structure, overview. The MTase domain of one subunit in dimeric RsmE is responsible for binding of one S-adenosyl-L-methionine molecule and catalytic process while the PUA-like domain in the other subunit is mainly responsible for recognition of one substrate molecule, the ribosomal RNA fragment and ribosomal protein complex. The methylation process is required by collaboration of both subunits, and dimerization is functionally critical for catalysis. Molecular replacement of crystal structure, PDB ID 1VHY |
720262 |
| 2.1.1.193 | physiological function |
RsmE is responsible for methylation of U1498 in 16S ribosomal RNA in Escherichia coli |
720262 |
