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Literature summary for 2.7.1.176 extracted from

  • Meinhart, A.; Alonso, J.C.; Straeter, N.; Saenger, W.
    Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation (2003), Proc. Natl. Acad. Sci. USA, 100, 1661-1666.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.176

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence comparisons Streptococcus pyogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and selenomethionine-derivated epsilon2/zeta2 protein complexes, X-ray diffraction structure determination and analysis at 1.95 A and 3.1 A resolution, respectively, multiple anomalous diffraction, modeling Streptococcus pyogenes

Protein Variants

Protein Variants Comment Organism
D67T site-directed mutagenesis Streptococcus pyogenes
K46A site-directed mutagenesis, the change in the Walker A motif enables cloning and expression of genes K46A and D67T in Escherichia coli without coexpression of the antagonistic gene epsilon Streptococcus pyogenes
K46A/D67T site-directed mutagenesis, the change in the Walker A motif enables cloning and expression of genes K46A and D67T in Escherichia coli without coexpression of the antagonistic gene epsilon Streptococcus pyogenes
additional information a mutant variant truncated after Val-234 lacks the helix K-loop-helix L appendage Streptococcus pyogenes
R158A site-directed mutagenesis, the mutant construct can be cloned into Escherichia coli but not overexpressed Streptococcus pyogenes
R158A/R171S site-directed mutagenesis, the mutant can be cloned and expressed Streptococcus pyogenes
R171S site-directed mutagenesis Streptococcus pyogenes

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes Q54944
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information free zeta acts as phosphotransferase by using ATP/GTP. In epsilon2zeta2, the toxin zeta is inactivated because the N-terminal helix of the antitoxin epsilon blocks the ATP/GTP-binding site, toxin-antitoxin interactions, overview Streptococcus pyogenes ?
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 ?

Synonyms

Synonyms Comment Organism
toxin zeta
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 Streptococcus pyogenes

Cofactor

Cofactor Comment Organism Structure
ATP
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 Streptococcus pyogenes
GTP
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 Streptococcus pyogenes

General Information

General Information Comment Organism
additional information the antitoxin toxin system epsilon/zeta and antibiotic resistance proteins are encoded on the broad-host-range, low-copy-number plasmid pSM19035. Theepsilon2/zeta2 protein complex is biologically nontoxic. The predominant contacts between antitoxin epsilon and toxin zeta involve helix a of epsilon, toxin-antitoxin interactions, overview Streptococcus pyogenes