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Literature summary for 3.4.21.88 extracted from
- 1.2.ANG.-resolution crystal structures reveal the second tetrahedral intermediates of streptogrisin B (SGPB) (2008), Biochim. Biophys. Acta, 1784, 319-334.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the ssDNA-RecA filament interacts with LexA and activates a self-cleaving activity in LexA | Escherichia coli |
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the LexA repressor plays a key role in the induction of the SOS response and its importance in regulating responses to stress suggests that it may be exploited as a drug target | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| full-length mutant forms show that the LexA linker region, from residues Gln70 to Glu74 is solvent exposed | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S119A | one subunit is well-ordered throughout and in the non-cleavable state, whereas the second subunit, whilst disordered in the amino-terminal domain, adopts the cleavable state in the carboxy-terminal domain | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | LexA protein is the repressor, which, during normal bacterial growth downregulates its own expression | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Cereibacter sphaeroides | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Pseudomonas aeruginosa | - |
- |
- |
| Staphylococcus aureus | - |
- |
- |
| Synechocystis sp. | - |
- |
- |
| Xanthomonas sp. | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | intact LexA dimerises by the carboxyterminal domain, and binds to DNA sequences via a helix-turn-helix in its amino-terminal domain. Upon self-cleavage between residues Ala84 and Gly85, LexA dissociates from its DNA targets (SOS boxes), causing the induction of the SOS regulon. Two distinct conformations of the LexA cleavage site region | Escherichia coli | ? | - |
? |  |
| additional information | LexA paralogue can activate transcription | Cereibacter sphaeroides | ? | - |
? | |
| additional information | LexA paralogue can activate transcription | Synechocystis sp. | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | free LexA is predominantly a dimer | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LexA | - |
Staphylococcus aureus |
| LexA | - |
Bacillus subtilis |
| LexA | - |
Escherichia coli |
| LexA | - |
Cereibacter sphaeroides |
| LexA | - |
Pseudomonas aeruginosa |
| LexA | - |
Xanthomonas sp. |
| LexA | - |
Synechocystis sp. |
| LexA transcriptional repressor | - |
Staphylococcus aureus |
| LexA transcriptional repressor | - |
Bacillus subtilis |
| LexA transcriptional repressor | - |
Escherichia coli |
| LexA transcriptional repressor | - |
Cereibacter sphaeroides |
| LexA transcriptional repressor | - |
Pseudomonas aeruginosa |
| LexA transcriptional repressor | - |
Xanthomonas sp. |
| LexA transcriptional repressor | - |
Synechocystis sp. |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Escherichia coli | - |
- |
6.5 |
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Release 2023.1 (January 2023)
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