A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein.
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.
Heilek
G M
GM
Tularik Inc., South San Francisco, California 94080, USA.
Peterson
M G
MG
D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000502:physiology; D043583:Nucleoside-Triphosphatase; D017354:Point Mutation; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000737:chemistry* / Q000502:physiology; D013329:Structure-Activity Relationship; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000502:physiology; D012697:Serine Endopeptidases; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
D017766:Acid Anhydride Hydrolases; D043583:Nucleoside-Triphosphatase; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases; D017361:Viral Nonstructural Proteins; C084422:NS3 protein, hepatitis C virus; D012697:Serine Endopeptidases; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases