Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 22, Issue 6, Pages 701-710Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2012.10.005
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Funding
- National Institutes of Health [GM54608]
- Department of Energy [DE-FG02-10ER16194]
- NASA [NNA08C-N85A]
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Enzymes in the radical SAM (RS) superfamily catalyze a wide variety of reactions through unique radical chemistry. The characteristic markers of the superfamily include a [4Fe-4S] cluster coordinated to the protein via a cysteine triad motif, typically CX3CX2C, with the fourth iron coordinated by S-adenosylmethionine (SAM). The SAM serves as a precursor for a 5'-deoxyadenosyl radical, the central intermediate in nearly all RS enzymes studied to date. The SAM-bound [4Fe-4S] cluster is located within a partial or full triosephosphate isomerase (TIM) barrel where the radical chemistry occurs protected from the surroundings. In addition to the TIM barrel and a RS [4Fe-4S] cluster, many members of the superfamily contain additional domains and/or additional Fe-S clusters. Recently characterized superfamily members are providing new examples of the remarkable range of reactions that can be catalyzed, as well as new structural and mechanistic insights into these fascinating reactions.
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