SPASM and Twitch Domains in S-Adenosylmethionine (SAM) Radical Enzymes
Author(s)Goldman, Peter J.; Drennan, Catherine L.; Grell, Tsehai Ariane
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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.
DepartmentMassachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of Chemistry
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology (ASBMB)
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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