Activating Compound | Comment | Organism | Structure |
---|---|---|---|
RNA | the ATPase activity is stimulated by the presence of RNA and single-stranded DNA molecules | West Nile virus | |
single-stranded DNA | the ATPase activity is stimulated by the presence of RNA and single-stranded DNA molecules | West Nile virus |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli, C-terminal portion with the ATPase/helicase domain, plasmid pET-30a | West Nile virus |
expression of the soluble His6-tagged C-terminal portion of NS3 in Escherichia coli C41 cells | West Nile virus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0095 | - |
ATP | pH 7.5, 37°C, native WNV NS3 protein purified from infected cells | West Nile virus | |
0.013 | - |
ATP | recombinant protein including C-terminal portion the ATPase/helicase domain encompassing residues 181-619, ATP concentration 1mM ATP, ATPase but not RNA helicase activity | West Nile virus | |
0.13 | - |
ATP | pH 7.5, 37°C, recombinant C-terminal portion of the NS3 | West Nile virus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates | West Nile virus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
66000 | - |
recombinant protein of C-terminal portion the ATPase/helicase domain, residues 181-619, SDS-PAGE, gel filtration | West Nile virus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | West Nile virus | - |
ADP + phosphate | - |
? | |
ATP + H2O | West Nile virus WNV | - |
ADP + phosphate | - |
? | |
additional information | West Nile virus | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication | ? | - |
? | |
additional information | West Nile virus WNV | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
West Nile virus | - |
WNV | - |
West Nile virus WNV | - |
WNV | - |
Purification (Comment) | Organism |
---|---|
gel filtration, recombinant protein, soluble form | West Nile virus |
recombinant soluble His6-tagged C-terminal portion of NS3 in Escherichia coli by nickel affinity chromatography and gel filtration | West Nile virus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
structural characterization of the C-terminal portion containing the ATPase/helicase domain, encompasses residues 181-619, monomer structure determined by analytical centrifugation and gel filtration, SDS-PAGE and immunoblotting, structure determined by circular dichroism and fluorescence spectroscopy, ATPase activity stimulated by RNA and ssDNA, no RNA helicase activity at protein concentrations up to 500 nM, linker region between the protease and the helicase domains predicted as a prerequisite for protein-protein interactions leading to the formation of the active oligomer | West Nile virus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
West Nile virus | ADP + phosphate | - |
? | |
ATP + H2O | recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities | West Nile virus | ADP + phosphate | - |
? | |
ATP + H2O | - |
West Nile virus WNV | ADP + phosphate | - |
? | |
ATP + H2O | recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities | West Nile virus WNV | ADP + phosphate | - |
? | |
additional information | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication | West Nile virus | ? | - |
? | |
additional information | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain | West Nile virus | ? | - |
? | |
additional information | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication | West Nile virus WNV | ? | - |
? | |
additional information | NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain | West Nile virus WNV | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration | West Nile virus |
monomer | in solution, x * 66000, about, recombinant soluble His6-tagged C-terminal portion of NS3, SDS-PAGE | West Nile virus |
More | the linker region plays a critical role in determining the protein-protein interactions that leads to the formation of the active oligomer | West Nile virus |
Synonyms | Comment | Organism |
---|---|---|
non-structural protein 3 | - |
West Nile virus |
nonstructural protein 3 | ambiguous | West Nile virus |
NS3 | - |
West Nile virus |
NS3 helicase | - |
West Nile virus |
NS3 NTPase/helicase | - |
West Nile virus |
NS3 NTPase/helicase | ambiguous | West Nile virus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | West Nile virus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | West Nile virus |