Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site.

@article{Li2009InhibitoryMO,
  title={Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site.},
  author={G. Li and Y Zhang and M. Inouye and Mitsuhiko Ikura},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 21},
  pages={14628-36}
}
In Escherichia coli, RelE toxin participates in growth arrest and cell death by inducing mRNA degradation at the ribosomal A-site under stress conditions. The NMR structures of a mutant of E. coli RelE toxin, RelE(R81A/R83A), with reduced toxicity and its complex with an inhibitory peptide from RelB antitoxin, RelB(C) (Lys(47)-Leu(79)), have been determined. In the free RelE(R81A/R83A) structure, helix alpha4 at the C terminus adopts a closed conformation contacting with the beta-sheet core and… CONTINUE READING

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RelB Inhibits RelE through a Helix Displacement 14636 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

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