Send to

Choose Destination
Curr Opin Struct Biol. 2002 Dec;12(6):783-93.

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

Author information

Centre for Drug Design and Development, and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia.

Erratum in

  • Curr Opin Struct Biol. 2003 Feb;13(1):142.


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.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center