Abstract
The NS3 protein of hepatitis C virus contains a bipartite structure consisting of an N-terminal serine protease and a C-terminal DEAD box helicase. We show that the C-terminal domain has ATPase and panhelicase activities. The integrity of the helicase function is dependent on the conserved DEAD motif and can be abolished by a His-Ala point mutation, leaving a fully functional nucleoside triphosphatase.
MeSH terms
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Acid Anhydride Hydrolases / chemistry*
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Acid Anhydride Hydrolases / physiology
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Nucleoside-Triphosphatase
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Point Mutation
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RNA Helicases
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RNA Nucleotidyltransferases / chemistry*
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RNA Nucleotidyltransferases / physiology
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Structure-Activity Relationship
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Viral Nonstructural Proteins / chemistry*
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Viral Nonstructural Proteins / physiology
Substances
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NS3 protein, hepatitis C virus
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Viral Nonstructural Proteins
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RNA Nucleotidyltransferases
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Acid Anhydride Hydrolases
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Nucleoside-Triphosphatase
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RNA Helicases