Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis

@article{Ding1996IdentificationOT,
  title={Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis},
  author={Xiaochun Ding and Huaqiang Zeng and N. Schiering and Dagmar Ringe and James Robert Murphy},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={382-387}
}
The diphtheria tox represser, DtxR, is a 226 amino acid transition metal ion-activated regulatory protein that controls the expression of diphtheria toxin in toxigenic Corynebacterium diphtheriae. The previously solved three-dimensional DtxR structures have identified two potential metal ion binding sites which may play a role in the activation of DNA binding by the represser. We have used both X-ray crystallographic and site-directed mutational analysis of DtxR(C102D)–Ni2+ complexes and DtxR… CONTINUE READING
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