Diphtheria toxin repressor: Difference between revisions

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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=''>


'''Diphtheria toxin repressor''' (DtxR) is an iron-dependent repressor which is synthesized by the diphtheria bacterium when it is in iron-poor environment.  DtxR structure contains a DNA-binding domain (DBD) containing the hlix-turn-helix motif at the N-terminal, an interface domain containing the metal-binding sites and a flexible C-terminal. The DtxR regulates the expression of high affinity iron uptake system. 
'''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>
 
== Structural highlights ==
 
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.
</StructureSection>
</StructureSection>


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**[[1c0w]] – CdDtxR + Co + DNA<br />
**[[1c0w]] – CdDtxR + Co + DNA<br />
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}}
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 16:10, 30 December 2015


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 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.

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

Drag the structure with the mouse to rotate

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

Updated on 30-December-2015

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky