Diphtheria toxin repressor
From Proteopedia
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- | <StructureSection load='1c0w' size='350' side='right' caption='Structure of diphtheria toxin repressor complex with DNA and Co+2 ion (PDB entry [[1c0w]])' scene=''> | + | <StructureSection load='1c0w' size='350' side='right' caption='Structure of diphtheria toxin repressor complex with DNA and Co+2 ion (PDB entry [[1c0w]])' scene='55/554905/Cv/1'> |
'''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. <ref>PMID:12675807</ref> | '''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. <ref>PMID:12675807</ref> |
Revision as of 15:16, 4 January 2016
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3D structures of diphtheria toxin repressor
Updated on 04-January-2016
References
- ↑ 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
- ↑ 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