1xcv

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(New page: 200px<br /><applet load="1xcv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xcv, resolution 2.10&Aring;" /> '''Crystal Structure Of...)
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[[Image:1xcv.gif|left|200px]]<br /><applet load="1xcv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xcv, resolution 2.10&Aring;" />
 
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'''Crystal Structure Of (H79AC102D)Dtxr complexed with Nickel(II)'''<br />
 
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==About this Structure==
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==Crystal Structure Of (H79AC102D)Dtxr complexed with Nickel(II)==
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1XCV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] with NI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XCV OCA].
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<StructureSection load='1xcv' size='340' side='right'caption='[[1xcv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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[[Category: Corynebacterium diphtheriae]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[1xcv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XCV FirstGlance]. <br>
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[[Category: Daquino, J.A.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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[[Category: Ringe, D.]]
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<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>
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[[Category: NI]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xcv OCA], [https://pdbe.org/1xcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xcv RCSB], [https://www.ebi.ac.uk/pdbsum/1xcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xcv ProSAT]</span></td></tr>
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[[Category: helix-turn-helix]]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xc/1xcv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xcv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The diphtheria toxin repressor (DtxR) is a metal ion-activated transcriptional regulator that has been linked to the virulence of Corynebacterium diphtheriae. Structure determination has shown that there are two metal ion binding sites per repressor monomer, and site-directed mutagenesis has demonstrated that binding site 2 (primary) is essential for recognition of the target DNA repressor, leaving the role of binding site 1 (ancillary) unclear. Calorimetric techniques have demonstrated that although binding site 1 (ancillary) has high affinity for metal ion with a binding constant of 2 x 10(-7), binding site 2 (primary) is a low-affinity binding site with a binding constant of 6.3 x 10(-4). These two binding sites act in an independent fashion, and their contribution can be easily dissected by traditional mutational analysis. Our results clearly demonstrate that binding site 1 (ancillary) is the first one to be occupied during metal ion activation, playing a critical role in stabilization of the repressor. In addition, structural data obtained for the mutants Ni-DtxR(H79A,C102D), reported here, and the previously reported DtxR(H79A) have allowed us to propose a mechanism of metal activation for DtxR.
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:59:57 2007''
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Mechanism of metal ion activation of the diphtheria toxin repressor DtxR.,D'Aquino JA, Tetenbaum-Novatt J, White A, Berkovitch F, Ringe D Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18408-13. Epub 2005 Dec 13. PMID:16352732<ref>PMID:16352732</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1xcv" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Diphtheria toxin repressor|Diphtheria toxin repressor]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Corynebacterium diphtheriae]]
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[[Category: Large Structures]]
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[[Category: D'aquino JA]]
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[[Category: Ringe D]]

Current revision

Crystal Structure Of (H79AC102D)Dtxr complexed with Nickel(II)

PDB ID 1xcv

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