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Literature summary extracted from

  • Lee, T.; James, M.N.
    1.2.ANG.-resolution crystal structures reveal the second tetrahedral intermediates of streptogrisin B (SGPB) (2008), Biochim. Biophys. Acta, 1784, 319-334.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.88 additional information the ssDNA-RecA filament interacts with LexA and activates a self-cleaving activity in LexA Escherichia coli

Application

EC Number Application Comment Organism
3.4.21.88 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)

EC Number Crystallization (Comment) Organism
3.4.21.88 full-length mutant forms show that the LexA linker region, from residues Gln70 to Glu74 is solvent exposed Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.88 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

EC Number Inhibitors Comment Organism Structure
3.4.21.88 additional information LexA protein is the repressor, which, during normal bacterial growth downregulates its own expression Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.88 Bacillus subtilis
-
-
-
3.4.21.88 Cereibacter sphaeroides
-
-
-
3.4.21.88 Escherichia coli
-
-
-
3.4.21.88 Pseudomonas aeruginosa
-
-
-
3.4.21.88 Staphylococcus aureus
-
-
-
3.4.21.88 Synechocystis sp.
-
-
-
3.4.21.88 Xanthomonas sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.88 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 ?
-
 ?
3.4.21.88 additional information LexA paralogue can activate transcription Cereibacter sphaeroides ?
-
 ?
3.4.21.88 additional information LexA paralogue can activate transcription Synechocystis sp. ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.88 dimer free LexA is predominantly a dimer Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.21.88 LexA
-
 Staphylococcus aureus
3.4.21.88 LexA
-
 Bacillus subtilis
3.4.21.88 LexA
-
 Escherichia coli
3.4.21.88 LexA
-
 Cereibacter sphaeroides
3.4.21.88 LexA
-
 Pseudomonas aeruginosa
3.4.21.88 LexA
-
 Xanthomonas sp.
3.4.21.88 LexA
-
 Synechocystis sp.
3.4.21.88 LexA transcriptional repressor
-
 Staphylococcus aureus
3.4.21.88 LexA transcriptional repressor
-
 Bacillus subtilis
3.4.21.88 LexA transcriptional repressor
-
 Escherichia coli
3.4.21.88 LexA transcriptional repressor
-
 Cereibacter sphaeroides
3.4.21.88 LexA transcriptional repressor
-
 Pseudomonas aeruginosa
3.4.21.88 LexA transcriptional repressor
-
 Xanthomonas sp.
3.4.21.88 LexA transcriptional repressor
-
 Synechocystis sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.21.88 Escherichia coli
-
-
 6.5