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Literature summary for 3.4.21.88 extracted from

  • Luo, Y.; Pfuetzner, R.A.; Mosiman, S.
    Crystal structure of LexA: A conformational switch for regulation of self-cleavage (2001), Cell, 106, 585-594.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutants G85D, S119A, L89P/Q92W/E152A/K156A, and tryptic fragments of mutants S119A and L89P/Q92W/E152A/K156A Escherichia coli

Protein Variants

Protein Variants Comment Organism
G85D change in cleavage site, that blocks autocleavage but has normal active site, crystallization data Escherichia coli
L89P/Q92W/E152A/K156A designed to trap protein in conformation required for cleavage. Crystallization data of tryptic fragment containing amino acids 68–202 Escherichia coli
S119A change in the active site, but normal cleavage site. Crystallization data of full length protein and of tryptic fragment containing amino acids 68–202 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification protein undergoes self-cleavage reaction that requires RecA protein or occurs spontaneously at high pH-value. Cleavage site has two distinct and highly ordered conformations Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of Ala84-/-Gly bond in repressor LexA oxyanion hole is formed by A84, S119, M118 Escherichia coli

Subunits

Subunits Comment Organism
dimer crystallization data, mutants G85D, S119A, L89P/Q92W/E152A/K156A Escherichia coli