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[[Image:1xcv.gif|left|200px]]<br /><applet load="1xcv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xcv, resolution 2.10&Aring;" />
'''Crystal Structure Of (H79AC102D)Dtxr complexed with Nickel(II)'''<br />


==About this Structure==
==Crystal Structure Of (H79AC102D)Dtxr complexed with Nickel(II)==
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 <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCV OCA].  
<StructureSection load='1xcv' size='340' side='right'caption='[[1xcv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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'>[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>
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xc/1xcv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xcv" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Diphtheria toxin repressor|Diphtheria toxin repressor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Daquino, J A.]]
[[Category: D'aquino JA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: NI]]
[[Category: helix-turn-helix]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:29 2008''

Latest revision as of 06:43, 23 August 2023

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

1xcv, resolution 2.10Å

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