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Literature summary extracted from

  • Luo, D.; Xu, T.; Watson, R.P.; Scherer-Becker, D.; Sampath, A.; Jahnke, W.; Yeong, S.S.; Wang, C.H.; Lim, S.P.; Strongin, A.; Vasudevan, S.G.; Lescar, J.
    Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein (2008), EMBO J., 27, 3209-3219.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.13 single-stranded DNA on single-stranded RNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis Dengue virus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.13 expression in Escherichia coli Dengue virus
3.6.4.13 expression of the His-tagged catalytic domain of the NS3 helicase domain from dengue virus serotype 4 in Escherichia coli strain BL21 Dengue virus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.4.13 hanging drop vapour diffusion method, crystallization of native enzyme, enzyme in complex with adenylyl imidodiphosphate, enzyme in complex with ADP, enzyme in complex with single-stranded RNA and enzyme in complex with single-stranded RNA and ADP Dengue virus
3.6.4.13 purified recombinant His-tagged catalytic domain of the NS3, hanging drop vapour diffusion method, at 13°C over a well solution containing 0.1M MES, pH 6.5, and 20% PEG 3350, X-ray diffraction structure determination and analysis. Crystals for the AMPPNP complex are obtained by cocrystallization of NS3h at 5 mg/ml with 5 mM MnCl2 and 5 mM AMPPNP using a precipitating solution containing 0.1M MES, pH 6.5, and 10% PEG 3350, at 13°C. Crystals with ADP are obtained by cocrystallization at a concentration of 2.5 mg/ml with 5 mM MnCl2 and 5 mM ADP in 0.1 M Tris-HCl, pH 7.0, and 7.5% PEG 3350 at 23°C, further preparation of ternary complexes,overview Dengue virus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.13 Mg2+ activates, binding complexes, overview Dengue virus

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.13 Dengue virus
-
-
-
3.6.4.13 Dengue virus
-
 serotype 4
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.13
-
 Dengue virus
3.6.4.13 recombinant His-tagged catalytic domain of the NS3 helicase domain from dengue virus serotype 4 from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration Dengue virus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.13 ATP + H2O
-
 Dengue virus ADP + phosphate
-
 ?
3.6.4.13 additional information conformational changes during ATP hydrolysis and RNA unwinding: on ssRNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. Determination of enzyme structure-function relationship of enzyme bound to single-stranded RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent, reaction mechanism and RNA recognition, overview. RNA-unwinding mechanism, overview Dengue virus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.4.13 NS3 helicase
-
 Dengue virus
3.6.4.13 NS3 protein
-
 Dengue virus