Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex.

@article{Schureck2014StructureOT,
  title={Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex.},
  author={Marc A. Schureck and Tatsuya Maehigashi and Stacey J. Miles and Jhomar Marquez and Shein Ei Cho and Rachel Erdman and Christine M Dunham},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 2},
  pages={1060-70}
}
Bacterial toxin-antitoxin (TA) systems regulate key cellular processes to promote cell survival during periods of stress. During steady-state cell growth, antitoxins typically interact with their cognate toxins to inhibit activity presumably by preventing substrate recognition. We solved two x-ray crystal structures of the Proteus vulgaris tetrameric HigB-(HigA)2-HigB TA complex and found that, unlike most other TA systems, the antitoxin HigA makes minimal interactions with toxin HigB. HigB… CONTINUE READING

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