Literature summary for 1.3.98.3 extracted from

Shaveta, G.; Shi, J.; Chow, V.T.; Song, J.
Structural characterization reveals that viperin is a radical S-adenosyl-L-methionine (SAM) enzyme (2010), Biochem. Biophys. Res. Commun., 391, 1390-1395.

Cloned(Commentary)

Cloned (Comment)	Organism
viperin from monocytic cells, DNA and amino acid sequence determination and analysis, expression of His-tagged full-length enzyme, and of His-tagged viperin (45-361) and viperin (214-361) in Escherichia coli strain BL21	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	[4Fe-4S] cluster	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies, solubilization by 8 M urea and purification by nickel affinity chromatography and gel filtration	Homo sapiens

Renatured (Commentary)

Renatured (Comment)	Organism
recombinant soluble His-tagged viperin (45-361) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies is solubilized by 8 M urea and further renaturated and purificated by nickel affinity chromatography and gel filtration. Reconstitution of the [4Fe-4S] cluster in Viperin residues 45-361, overview	Homo sapiens

Renatured (Comment)

Organism

recombinant soluble His-tagged viperin (45-361) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies is solubilized by 8 M urea and further renaturated and purificated by nickel affinity chromatography and gel filtration. Reconstitution of the [4Fe-4S] cluster in Viperin residues 45-361, overview

Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
monocyte	-	Homo sapiens	-

Subunits

Subunits	Comment	Organism
More	structure analysis of recombinant His-tagged viperin (214-361) by UV-visible, circular dichroism, and NMR spectroscopy, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
viperin	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Homo sapiens
[4Fe-4S]-center	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	viperin is an interferon-inducible protein inhibiting a diverse spectrum of 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 enzymes. The radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin	Homo sapiens