SPASM and Twitch Domains in S-Adenosylmethionine (SAM) Radical Enzymes
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Author(s)
Goldman, Peter J.
Grell, Tsehai Ariane
Drennan, Catherine L
Date Issued
December 2014
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry and Molecular Biology (ASBMB)
Citation
Grell, Tsehai A. J., Peter J. Goldman, and Catherine L. Drennan. “SPASM and Twitch Domains in S-Adenosylmethionine (SAM) Radical Enzymes.” J. Biol. Chem. 290, no. 7 (December 4, 2014): 3964–3971.
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Author's final manuscript
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1074/jbc.R114.581249
