Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site.

@article{Das2004CrystalSO,
  title={Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site.},
  author={Kalyan Das and Thomas Acton and Yiwen Chiang and Lydia Shih and Eddy Arnold and Gaetano T. Montelione},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 12},
  pages={4041-6}
}
The RlmA class of enzymes (RlmA(I) and RlmA(II)) catalyzes N1-methylation of a guanine base (G745 in Gram-negative and G748 in Gram-positive bacteria) of hairpin 35 of 23S rRNA. We have determined the crystal structure of Escherichia coli RlmA(I) at 2.8-A resolution, providing 3D structure information for the RlmA class of RNA methyltransferases. The dimeric protein structure exhibits features that provide new insights into its molecular function. Each RlmA(I) molecule has a Zn-binding domain… CONTINUE READING
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Proteins Struct

  • J. Liu, H. Hegyi, T. B. Acton, G. T. Montelione, B. Rost
  • 2003

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