SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
Author(s)
Martin, JL
McMillan, FM
Griffith University Author(s)
Year published
2002
Metadata
Show full item recordAbstract
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 uncharacterised proteins and two proteins that lack methyltransferase activity.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 uncharacterised proteins and two proteins that lack methyltransferase activity.
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Journal Title
Current Opinion in Structural Biology
Volume
12
Issue
6
Subject
Medicinal and biomolecular chemistry
Biochemistry and cell biology
Biochemistry and cell biology not elsewhere classified