Structural studies of viperin, an antiviral radical SAM enzyme

Fenwick, Michael K.; Li, Yue; Cresswell, Peter; Modis, Yorgo; Ealick, Steven E.

doi:10.1073/pnas.1705402114

Title: Structural studies of viperin, an antiviral radical SAM enzyme

Journal Article · Mon Jun 12 00:00:00 EDT 2017 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1705402114· OSTI ID:1374624

Fenwick, Michael K. ^[1]; Li, Yue ^[2]; Cresswell, Peter ^[2];

^[3]; Ealick, Steven E. ^[1]

Cornell Univ., Ithaca, NY (United States)
Yale Univ. School of Medicine, New Haven, CT (United States)
Univ. of Cambridge (United Kingdom)

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. As a result, 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.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-06CH11357; DK067081; GM102869

OSTI ID:: 1374624

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Vol. 114, Issue 26; ISSN 0027-8424

Publisher:: National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Title: Structural studies of viperin, an antiviral radical SAM enzyme

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