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PMID: 12504684 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

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

Current opinion in structural biology ·Vol. 12 ·No. 6 ·2002-12-00 ·Pages 783-93

Martin JL, McMillan FM

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 uncharacterized proteins and two proteins that lack methyltransferase activity.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Humans Methyltransferases/chemistry,metabolism Models, Molecular Molecular Sequence Data Molecular Structure Protein Folding Protein Structure, Secondary S-Adenosylmethionine/metabolism Sequence Alignment
Chemicals
S-Adenosylmethionine Methyltransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Martin Jennifer L
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. J.Martin@imb.uq.edu.au
McMillan Fiona M
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2002-12-00
Pages
783-93
Language
English
Region
England
NLM ID
9107784
Subset
IM
Corrections
ErratumIn
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