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Literature summary for 3.6.4.13 extracted from

  • Feito, M.J.; Gomez-Gutierrez, J.; Ayora, S.; Alonso, J.C.; Peterson, D.; Gavilanes, F.
    Insights into the oligomerization state-helicase activity relationship of West Nile virus NS3 NTPase/helicase (2008), Virus Res., 135, 166-174.
    View publication on PubMed
Search for more literature for 3.6.4.13

Activating Compound

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(Commentary)

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 [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

Metals/Ions Comment Organism Structure
Mg2+ activates West Nile virus

Molecular Weight [Da]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
West Nile virus
-
 WNV
-
West Nile virus WNV
-
 WNV
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at West Nile virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at West Nile virus