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• W2625271458 endingPage "6811" @default.
• W2625271458 startingPage "6806" @default.
• W2625271458 abstract "Viperin is an IFN-inducible radical S-adenosylmethionine (SAM) enzyme that inhibits viral replication. We determined crystal structures of an anaerobically prepared fragment of mouse viperin (residues 45-362) complexed with S-adenosylhomocysteine (SAH) or 5'-deoxyadenosine (5'-dAdo) and l-methionine (l-Met). Viperin contains a partial (βα)6-barrel fold with a disordered N-terminal extension (residues 45-74) and a partially ordered C-terminal extension (residues 285-362) that bridges the partial barrel to form an overall closed barrel structure. Cys84, Cys88, and Cys91 located after the first β-strand bind a [4Fe-4S] cluster. The active site architecture of viperin with bound SAH (a SAM analog) or 5'-dAdo and l-Met (SAM cleavage products) is consistent with the canonical mechanism of 5'-deoxyadenosyl radical generation. The viperin structure, together with sequence alignments, suggests that vertebrate viperins are highly conserved and that fungi contain a viperin-like ortholog. Many bacteria and archaebacteria also express viperin-like enzymes with conserved active site residues. Structural alignments show that viperin is similar to several other radical SAM enzymes, including the molybdenum cofactor biosynthetic enzyme MoaA and the RNA methyltransferase RlmN, which methylates specific nucleotides in rRNA and tRNA. The viperin putative active site contains several conserved positively charged residues, and a portion of the active site shows structural similarity to the GTP-binding site of MoaA, suggesting that the viperin substrate may be a nucleoside triphosphate of some type." @default.
• W2625271458 created "2017-06-23" @default.
• W2625271458 creator A5019164857 @default.
• W2625271458 creator A5044367029 @default.
• W2625271458 creator A5046067654 @default.
• W2625271458 creator A5065397632 @default.
• W2625271458 creator A5078535260 @default.
• W2625271458 date "2017-06-12" @default.
• W2625271458 modified "2023-10-05" @default.
• W2625271458 title "Structural studies of viperin, an antiviral radical SAM enzyme" @default.
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• W2625271458 doi "https://doi.org/10.1073/pnas.1705402114" @default.
• W2625271458 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5495270" @default.
• W2625271458 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28607080" @default.
• W2625271458 hasPublicationYear "2017" @default.
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