Diphtheria toxin repressor

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Diphtheria toxin repressor (DtxR) is an iron-dependent repressor which is synthesized by the diphtheria bacterium when it is in iron-poor environment. The DtxR regulates the expression of high affinity iron uptake system. [1]

Structural highlights

DtxR structure contains an which contains , dimerization and metal-binding residues. DtxR contains .

  • .
  • .

A C-terminal domain folds into SH3-like conformation.[2]

Structure of diphtheria toxin repressor complex with DNA and Co+2 ion (PDB entry 1c0w)

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3D structures of diphtheria toxin repressor3D structures of diphtheria toxin repressor

Updated on 24-February-2019

ReferencesReferences

  1. Guedon E, Helmann JD. Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators. Mol Microbiol. 2003 Apr;48(2):495-506. PMID:12675807
  2. Pohl E, Holmes RK, Hol WG. Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J Mol Biol. 1999 Sep 24;292(3):653-67. PMID:10497029 doi:10.1006/jmbi.1999.3073

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