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Literature summary for 3.4.21.88 extracted from
- Structural insights into bacteriophage GIL01 gp7 inhibition of host LexA repressor (2019), Structure, 27, 1094-1102 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| RecA | RecA binds to and polymerizes on single-stranded DNA, which is a product of DNA damage. As a complex, it activates the autocleavage of LexA thereby lifting repression of SOS genes under DNA-damage conditions | [Bacillus thuringiensis] serovar konkukian |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
gel filtration | [Bacillus thuringiensis] serovar konkukian |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | [Bacillus thuringiensis] serovar konkukian | LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain | ? | - |
? |  |
| additional information | [Bacillus thuringiensis] serovar konkukian 97-27 | LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| [Bacillus thuringiensis] serovar konkukian | Q6HFB0 | - |
- |
| [Bacillus thuringiensis] serovar konkukian 97-27 | Q6HFB0 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | RecA binds to and polymerizes on single-stranded DNA, which is a product of DNA damage. As a complex, it activates the autocleavage of LexA thereby lifting repression of SOS genes under DNA-damage conditions | [Bacillus thuringiensis] serovar konkukian |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain | [Bacillus thuringiensis] serovar konkukian | ? | - |
? | |
| additional information | LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain | [Bacillus thuringiensis] serovar konkukian 97-27 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 26000, SDS-PAGE | [Bacillus thuringiensis] serovar konkukian |
| More | a monodisperse mixture of gp7 and LexA appears as a 72-kDa heterohexameric complex composed of a tetrameric gp7 and dimeric LexA | [Bacillus thuringiensis] serovar konkukian |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LexA | - |
[Bacillus thuringiensis] serovar konkukian |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | a monodisperse mixture of gp7 and LexA appears as a 72-kDa heterohexameric complex composed of a tetrameric gp7 and dimeric LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry | [Bacillus thuringiensis] serovar konkukian |
| physiological function | LexA is a central repressor in the SOS response. During infection of Bacillus thuringiensis with GIL01 bacteriophage, bacterial LexA represses the SOS response and the phage lytic cycle by binding DNA, the interaction is further stabilized upon binding of a viral protein, phage-borne gp7. Analysis of binding stoichiometry and potential interaction with LexA using surface plasmon resonance, static light scattering, and small-angle X-ray scattering, overview. LexA binds and represses expression through binding of dinBox1/1b, with LexA affinity for this region increased through interaction with a viral accessory protein gp7. Removal of the last six C-terminal residues of gp7 does not prevent its interaction with LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry. Under regular growth conditions, LexA binds SOS-box sequences upstream of DNA repair genes to suppress the expression of these genes | [Bacillus thuringiensis] serovar konkukian |
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