Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes |
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| Affiliation: | 1. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA;2. Department of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA;1. The Chemistry of Life Processes Institute, Northwestern University, Evanston, IL, USA;2. Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI, USA;3. Department of Chemistry, Michigan State University, East Lansing, MI, USA;4. Department of Molecular Biosciences, Northwestern University, Evanston, IL, USA;5. Department of Chemistry, Northwestern University, Evanston, IL, USA;6. Elemental Health Institute, Michigan State University, East Lansing, MI, USA;1. Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA;2. Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA;3. Howard Hughes Medical Institute, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA |
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| Abstract: | Radical S-adenosylmethionine (SAM) enzymes use a common catalytic core for diverse transformations. While all radical SAM enzymes bind a Fe4S4 cluster via a characteristic tri-cysteine motif, many bind additional metal cofactors. Recently reported structures of radical SAM enzymes that use methylcobalamin or additional iron-sulfur clusters as cosubstrates show that these auxiliary units are anchored by N- and C-terminal domains that vary significantly in size and topology. Despite this architectural diversity, all use a common surface for auxiliary cofactor docking. In the sulfur insertion and metallocofactor assembly systems evaluated here, interaction with iron-sulfur cluster assembly proteins or downstream scaffold proteins is an important component of catalysis. Structures of these complexes represent important new frontiers in structural analysis of radical SAM enzymes. |
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| Keywords: | Iron-sulfur cluster Cobalamin SAM Methylation Sulfur insertion Nitrogenase |
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