Diphtheria toxin repressor: Difference between revisions
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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. A C-terminal domain folds into SH3-like conformation. DtxR contains 2 metal binding sites.<ref>PMID:10497029</ref> | DtxR structure contains an <scene name='55/554905/Cv/2'>N-terminal domain</scene> 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 18:25, 4 January 2016
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 highlightsDtxR structure contains an 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.[2] |
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3D structures of diphtheria toxin repressor3D structures of diphtheria toxin repressor
Updated on 04-January-2016
ReferencesReferences
- ↑ 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