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      A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein.

      Journal of Biology

      physiology, chemistry, Viral Nonstructural Proteins, Structure-Activity Relationship, RNA Nucleotidyltransferases, RNA Helicases, Point Mutation, Nucleoside-Triphosphatase, Acid Anhydride Hydrolases

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          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.

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          Journal
          191896
          9223530

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