Structural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme

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Author(s)

  • Goyal Shaveta
  • Jiahai Shi
  • Vincent T.K. Chow
  • Jianxing Song

Detail(s)

Original languageEnglish
Pages (from-to)1390-1395
Journal / PublicationBiochemical and Biophysical Research Communications
Volume391
Issue number3
Publication statusPublished - 15 Jan 2010
Externally publishedYes

Abstract

Viperin is an interferon-inducible protein inhibiting many DNA and RNA viruses. It contains an N-terminal transmembrane helix, a highly conserved C-terminus and a middle region carrying a CX3CX2C motif, characteristic of radical S-adenosyl-l-methionine (SAM) enzymes. So far no structural characterization has been reported and reconstitution of the [4Fe-4S] cluster in viperin all failed. Here, by dissecting the 361-residue human viperin into 12 fragments, followed by extensive CD and NMR characterization, Viperin (45-361) was identified to be soluble and structured in buffers. Most importantly, we have successfully reconstituted the [4Fe-4S] cluster in Viperin (45-361), thus providing the first experimental evidence confirming that viperin is indeed a radical SAM enzyme. Furthermore, the C-terminus Viperin (214-361) which is insoluble in buffers but again can be solubilized in salt-free water appears to be only partially folded. Our results thus imply that the radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin. © 2009 Elsevier Inc. All rights reserved.

Research Area(s)

  • Circular dichroism spectroscopy, Interferon, Iron-sulfur cluster, NMR spectroscopy, Radical S-adenosyl-l-methionine (SAM) enzyme, Viperin

Citation Format(s)