Crystal structure of the Escherichia coli 23S rRNA:m5C methyltransferase RlmI (YccW) reveals evolutionary links between RNA modification enzymes.

@article{Sunita2008CrystalSO,
  title={Crystal structure of the Escherichia coli 23S rRNA:m5C methyltransferase RlmI (YccW) reveals evolutionary links between RNA modification enzymes.},
  author={Swain Sunita and Karolina L. Tkaczuk and Elzbieta Purta and Joanna M. Kasprzak and S. Douthwaite and Janusz M. Bujnicki and J. Sivaraman},
  journal={Journal of molecular biology},
  year={2008},
  volume={383 3},
  pages={652-66}
}
Methylation is the most common RNA modification in the three domains of life. Transfer of the methyl group from S-adenosyl-l-methionine (AdoMet) to specific atoms of RNA nucleotides is catalyzed by methyltransferase (MTase) enzymes. The rRNA MTase RlmI (rRNA large subunit methyltransferase gene I; previously known as YccW) specifically modifies Escherichia coli 23S rRNA at nucleotide C1962 to form 5-methylcytosine. Here, we report the crystal structure of RlmI refined at 2 A to a final R-factor… CONTINUE READING

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