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

    Author(s)
    Martin, JL
    McMillan, FM
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    2002
    Metadata
    Show full item record
    Abstract
    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
    DOI
    https://doi.org/10.1016/S0959-440X(02)00391-3
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Biochemistry and cell biology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/347884
    Collection
    • Journal articles

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