Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance

Nat Struct Biol. 1997 Jun;4(6):483-9. doi: 10.1038/nsb0697-483.


The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology*
  • Binding Sites
  • Drug Design
  • Drug Resistance, Microbial / physiology*
  • Enzyme Inhibitors / chemistry
  • Lincosamides
  • Macrolides / pharmacology
  • Magnetic Resonance Spectroscopy / methods
  • Methyltransferases / chemistry*
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Sequence Homology, Amino Acid
  • Virginiamycin / pharmacology


  • Anti-Bacterial Agents
  • Enzyme Inhibitors
  • Lincosamides
  • Macrolides
  • Virginiamycin
  • Methyltransferases
  • rRNA (adenosine-O-2'-)methyltransferase