SPASM and Twitch Domains in S-Adenosylmethionine (SAM) Radical Enzymes

S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate isomerase (TIM) barrel fold with N- and C-terminal extensions that tailor the structure of the enzyme to its specific functi...

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Bibliographic Details
Published in:The Journal of biological chemistry 2015-02, Vol.290 (7), p.3964-3971
Main Authors: Grell, Tsehai A.J., Goldman, Peter J., Drennan, Catherine L.
Format: Article
Language:English
Subjects:
AdoMet
Animals
Coenzymes - metabolism
Free Radicals - chemistry
Humans
Iron-Sulfur Protein
Iron-Sulfur Proteins - metabolism
Metalloproteins - metabolism
Methylation
Minireviews
Molybdenum Cofactors
Post-translational Modification (PTM)
Protein Methyltransferases - metabolism
Protein Structure, Tertiary
Pteridines - metabolism
Radical
S-Adenosylmethionine (SAM)
S-Adenosylmethionine - chemistry
S-Adenosylmethionine - metabolism
Structural Biology
Sulfatases - metabolism
Triose-Phosphate Isomerase - metabolism
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Summary:S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate isomerase (TIM) barrel fold with N- and C-terminal extensions that tailor the structure of the enzyme to its specific function. One extension, termed a SPASM domain, binds two auxiliary [4Fe-4S] clusters and is present within peptide-modifying enzymes. The first structure of a SPASM-containing enzyme, anaerobic sulfatase-maturating enzyme (anSME), revealed unexpected similarities to two non-SPASM proteins, butirosin biosynthetic enzyme 2-deoxy-scyllo-inosamine dehydrogenase (BtrN) and molybdenum cofactor biosynthetic enzyme (MoaA). The latter two enzymes bind one auxiliary cluster and exhibit a partial SPASM motif, coined a Twitch domain. Here we review the structure and function of auxiliary cluster domains within the SAM radical enzyme superfamily.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.R114.581249