SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold

Curr Opin Struct Biol. 2002 Dec;12(6):783-93. doi: 10.1016/s0959-440x(02)00391-3.


The S-adenosylmethionine-dependent methyltransferase enzymes share little sequence identity, but incorporate a highly conserved structural fold. Surprisingly, residues that bind the common cofactor are poorly conserved, although the binding site is localised to the same region of the fold. The substrate-binding region of the fold varies enormously. Over the past two years, there has been a significant increase in the number of structures that are known to incorporate this fold, including several uncharacterized proteins and two proteins that lack methyltransferase activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Humans
  • Methyltransferases / chemistry*
  • Methyltransferases / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Folding*
  • Protein Structure, Secondary*
  • S-Adenosylmethionine / metabolism*
  • Sequence Alignment


  • S-Adenosylmethionine
  • Methyltransferases