Structure of the manganese-bound manganese transport regulator of Bacillus subtilis

@article{Glasfeld2003StructureOT,
  title={Structure of the manganese-bound manganese transport regulator of Bacillus subtilis},
  author={Arthur Glasfeld and Emmanuel Guedon and John D. Helmann and Richard G. Brennan},
  journal={Nature Structural Biology},
  year={2003},
  volume={10},
  pages={652-657}
}
The Bacillus subtilis manganese transport regulator, MntR, binds Mn2+ as an effector and is a repressor of transporters that import manganese. A member of the diphtheria toxin repressor (DtxR) family of metalloregulatory proteins, MntR exhibits selectivity for Mn2+ over Fe2+. Replacement of a metal-binding residue, Asp8, with methionine (D8M) relaxes this specificity. We report here the X-ray crystal structures of wild-type MntR and the D8M mutant bound to manganese with 1.75 Å and 1.61… 

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