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| | ==DIPHTHERIA TOX REPRESSOR (C102D MUTANT) COMPLEXED WITH NICKEL== | | ==DIPHTHERIA TOX REPRESSOR (C102D MUTANT) COMPLEXED WITH NICKEL== |
| - | <StructureSection load='2tdx' size='340' side='right' caption='[[2tdx]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='2tdx' size='340' side='right'caption='[[2tdx]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2tdx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tdx 1tdx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2TDX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2tdx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tdx 1tdx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TDX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DTXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1717 "Bacillus diphtheriae" Kruse in Flugge 1886])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2tdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tdx OCA], [http://pdbe.org/2tdx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2tdx RCSB], [http://www.ebi.ac.uk/pdbsum/2tdx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2tdx ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2tdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tdx OCA], [https://pdbe.org/2tdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tdx RCSB], [https://www.ebi.ac.uk/pdbsum/2tdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tdx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DTXR_CORDI DTXR_CORDI]] Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess. | + | [https://www.uniprot.org/uniprot/DTXR_CORDI DTXR_CORDI] Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus diphtheriae kruse in flugge 1886]] | + | [[Category: Corynebacterium diphtheriae]] |
| - | [[Category: Ding, X]] | + | [[Category: Large Structures]] |
| - | [[Category: Murphy, J R]] | + | [[Category: Ding X]] |
| - | [[Category: Ringe, D]] | + | [[Category: Murphy JR]] |
| - | [[Category: Schiering, N]] | + | [[Category: Ringe D]] |
| - | [[Category: White, A]] | + | [[Category: Schiering N]] |
| - | [[Category: Zheng, H]] | + | [[Category: White A]] |
| - | [[Category: Diphtheria tox repressor]]
| + | [[Category: Zheng H]] |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Dna-binding regulatory protein]]
| + | |
| - | [[Category: Iron-regulated repressor]]
| + | |
| - | [[Category: Transcription regulation]]
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| Structural highlights
Function
DTXR_CORDI Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The virulent phenotype of the pathogenic bacterium Corynebacterium diphtheriae is conferred by diphtheria toxin, whose expression is an adaptive response to low concentrations of iron. The expression of the toxin gene (tox) is regulated by the repressor DtxR, which is activated by transition metal ions. X-ray crystal structures of DtxR with and without (apo-form) its coordinated transition metal ion have established the general architecture of the repressor, identified the location of the metal-binding sites, and revealed a metal-ion-triggered subunit-subunit 'caliper-like' conformational change. Here we report the three-dimensional crystal structure of the complex between a biologically active Ni(II)-bound DtxR(C102D) mutant, in which a cysteine is replaced by an aspartate at residue 102, and a 33-base-pair DNA segment containing the toxin operator toxO. This structure shows that DNA interacts with two dimeric repressor proteins bound to opposite sides of the tox operator. We propose that a metal-ion-induced helix-to-coil structural transition in the amino-terminal region of the protein is partly responsible for the unique mode of repressor activation by transition metal ions.
Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex.,White A, Ding X, vanderSpek JC, Murphy JR, Ringe D Nature. 1998 Jul 30;394(6692):502-6. PMID:9697776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ White A, Ding X, vanderSpek JC, Murphy JR, Ringe D. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature. 1998 Jul 30;394(6692):502-6. PMID:9697776 doi:10.1038/28893
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