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Diphtheria toxin repressor

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== Structural highlights ==
== Structural highlights ==
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DtxR structure contains a DNA-binding domain (DBD) containing the helix-turn-helix motif at the N-terminal, an interface domain containing the metal-binding sites and a flexible C-terminal.
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DtxR structure contains an N-terminal domain which contains DNA-binding domain (DBD) with a helix-turn-helix motif, dimerization and metal-binding residues. A C-terminal domain folds into SH3-like conformation. DtxR contains 2 metal binding sites.<ref>PMID:10497029</ref>
</StructureSection>
</StructureSection>

Revision as of 13:40, 30 December 2015

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

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3D structures of diphtheria toxin repressor

Updated on 30-December-2015

References

  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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Michal Harel, Alexander Berchansky

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