Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2009.12.070
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dc.titleStructural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme
dc.contributor.authorShaveta, G.
dc.contributor.authorSong, J.
dc.contributor.authorShi, J.
dc.contributor.authorChow, V.T.K.
dc.date.accessioned2011-11-29T06:11:08Z
dc.date.available2011-11-29T06:11:08Z
dc.date.issued2010
dc.identifier.citationShaveta, G., Song, J., Shi, J., Chow, V.T.K. (2010). Structural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme. Biochemical and Biophysical Research Communications 391 (3) : 1390-1395. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2009.12.070
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28929
dc.description.abstractViperin 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2009.12.070
dc.sourceScopus
dc.subjectCircular dichroism spectroscopy
dc.subjectInterferon
dc.subjectIron-sulfur cluster
dc.subjectNMR spectroscopy
dc.subjectRadical S-adenosyl-l-methionine (SAM) enzyme
dc.subjectViperin
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/j.bbrc.2009.12.070
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume391
dc.description.issue3
dc.description.page1390-1395
dc.description.codenBBRCA
dc.identifier.isiut000274097800017
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