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Epsilon antitoxin

From Wikipedia, the free encyclopedia
Bacterial epsilon antitoxin
crystal structure of the plasmid maintenance system epsilon/zeta: meachnism of toxin inactivation and toxin function
Identifiers
SymbolEpsilon_antitox
PfamPF08998
InterProIPR015090
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the epsilon antitoxin, produced by various prokaryotes, forms part of a post-segregational killing system, which is involved in the initiation of programmed cell death of plasmid-free cells. The protein is folded into a three-helix bundle that directly interacts with the zeta toxin, inactivating it.[1]

References

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  1. ^ Meinhart A, Alonso JC, Strater N, Saenger W (February 2003). "Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation". Proc. Natl. Acad. Sci. U.S.A. 100 (4): 1661–6. doi:10.1073/pnas.0434325100. PMC 149889. PMID 12571357.
This article incorporates text from the public domain Pfam and InterPro: IPR015090