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='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>
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 == 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.
+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>.
+A C-terminal domain folds into SH3-like conformation.<ref>PMID:10497029</ref>
 </StructureSection>