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> | ||
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== Structural highlights == | == Structural highlights == | ||
| - | DtxR structure contains an N-terminal domain which contains DNA-binding domain (DBD) with a helix-turn-helix motif, dimerization and metal-binding residues. | + | DtxR structure contains an <scene name='55/554905/Cv/7'>N-terminal domain</scene> which contains <scene name='55/554905/Cv/8'>DNA-binding domain (DBD) with a helix-turn-helix motif</scene>, dimerization and metal-binding residues. DtxR contains <scene name='55/554905/Cv/9'>2 metal binding sites</scene>. |
| + | *<scene name='55/554905/Cv/10'>First metal binding site</scene>. | ||
| + | *<scene name='55/554905/Cv/11'>Second metal binding site</scene>. | ||
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| + | A C-terminal domain folds into SH3-like conformation.<ref>PMID:10497029</ref> | ||
</StructureSection> | </StructureSection> | ||
Current revision
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3D structures of diphtheria toxin repressor
Updated on 24-February-2019
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
