Literature summary for 3.4.21.88 extracted from

Sousa, F.J.; Lima, L.M.; Pacheco, A.B.; Oliveira, C.L.; Torriani, I.; Almeida, D.F.; Foguel, D.; Silva, J.L.; Mohana-Borges, R.
Tetramerization of the LexA repressor in solution: implications for gene regulation of the E.coli SOS system at acidic pH (2006), J. Mol. Biol., 359, 1059-1074.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
25000	-	4 * 25000 at pH 2.5, oligomerization at acidic pH	Escherichia coli
100000	-	tetramer, pore-limiting Page at pH 2.5	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
of the recombinant protein	Escherichia coli

Subunits

Subunits	Comment	Organism
dimer	at pH 7.2	Escherichia coli
More	structure of the LexA tetramer is analysed by fluorescence spectroscopy and light-scattering measurements, circular dichroism experiments, NMR and small angle X-ray scattering analysis, LexA forms tetramers at pH4 but not at pH2.5, LexA repressor is the key regulatory protein of the DNA repair system, the SOS response. When DNA damage occurs, LexA repressor is inactivated by separating its N and C-terminal domains in a pH dependent manner	Escherichia coli
tetramer	4 * 25000 at pH 2.5, oligomerization at acidic pH	Escherichia coli

Synonyms

Synonyms	Comment	Organism
LexA protein	-	Escherichia coli
LexA repressor	-	Escherichia coli

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Release 2023.1 (January 2023)