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Literature summary for 5.6.2.3 extracted from
- Biochemical characterization of a mycobacteriophage derived DnaB ortholog reveals new insight into the evolutionary origin of DnaB helicases (2015), PLoS ONE, 10, e0134762.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene 80 encoding WCGp80, phylogenetic and evolutionary analysis, cloning in Escherichia coli strains XL1-BLUE and M15, recombinant His6-tagged enzyme expression in Escherichia coli strain Bl21(DE3) | Fromanvirus D29 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K201A | site-directed mutagenesis | Fromanvirus D29 |
| additional information | construction of a thioredoxin-tagged truncated version of WCGp80 protein, thio-DELTAN(1-189)WCGp80, in which the N-terminal sequences are removed, the mutant is fully capable of supporting helicase activity, although its ATP-dependence properties are altered, the substrate saturation curve for ATP in case of the mutant derivative is hyperbolic | Fromanvirus D29 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | cooperative binding of ATP | Fromanvirus D29 |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Fromanvirus D29 |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52000 | - |
6 * 52000, SDS-PAGE | Fromanvirus D29 |
| 318000 | - |
recombinant enzyme, gel filtration | Fromanvirus D29 |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Fromanvirus D29 | - |
ADP + phosphate | - |
? | |
| additional information | Fromanvirus D29 | enzyme WCGp80 unwinds DNA in a 5'-3' direction at replication forks in an ATP-dependent manner. DnaB helicases prefer forks as substrates | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Fromanvirus D29 | Q19XY0 | gene 80 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Fromanvirus D29 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Fromanvirus D29 | ADP + phosphate | - |
? | |
| ATP + H2O | enzyme WCGp80 is an ATP-dependent 5'->3' helicase showing low activity with the 5' 23-nt ssDNA tailed fork | Fromanvirus D29 | ADP + phosphate | - |
? | |
| additional information | enzyme WCGp80 unwinds DNA in a 5'-3' direction at replication forks in an ATP-dependent manner. DnaB helicases prefer forks as substrates | Fromanvirus D29 | ? | - |
? | |
| additional information | no activity with AMP-PNP | Fromanvirus D29 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 52000, SDS-PAGE | Fromanvirus D29 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DnaB class helicase | - |
Fromanvirus D29 |
| DnaB helicase | - |
Fromanvirus D29 |
| DnaB type helicase | - |
Fromanvirus D29 |
| WCGp80 | - |
Fromanvirus D29 |
| Wildcat Gp80 | - |
Fromanvirus D29 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Fromanvirus D29 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8 | assay at | Fromanvirus D29 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | DnaB are considered to be members of the RecA superfamily. All members of this superfamily, including DnaB, have a conserved C-terminal domain, known as the RecA core. DnaB helicases of the DnaB helicase family may have evolved from single domain RecA core proteins having helicase activities of their own, through the incorporation of additional N-terminal sequences. The helicases can be classified into six super-families of which DnaB which is the replicative helicase in Eubacteria, belongs to Superfamily 4. DnaB helicases are characteristically hexameric in structure. phylogenetic and evolutionary analysis identifies WCGp80 to be related to an ancestor of DnaB helicase family proteins | Fromanvirus D29 |
| additional information | the DnaB helicase activity is primarily a function of the RecA core although additional N-terminal sequences may be necessary for fine tuning its activity and stability. WCGp80, like several other DnaB helicases, possess tryptophanyl residues within the RecA core region | Fromanvirus D29 |
| physiological function | the primary function of DNA helicases is to act as motor proteins to unwind double-stranded DNA, RNA and DNA-RNA hybrids. The energy required for this purpose is derived from the hydrolysis of NTP. DnaB helicases are characteristically hexameric in structure and unwind DNA in an unidirectional manner in the 5'-3' direction | Fromanvirus D29 |
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