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2xig

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<StructureSection load='2xig' size='340' side='right'caption='[[2xig]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='2xig' size='340' side='right'caption='[[2xig]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xig]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XIG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XIG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xig]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XIG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.85&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xig OCA], [http://pdbe.org/2xig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xig RCSB], [http://www.ebi.ac.uk/pdbsum/2xig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xig ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=2xig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xig OCA], [https://pdbe.org/2xig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xig RCSB], [https://www.ebi.ac.uk/pdbsum/2xig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xig ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FUR_HELPY FUR_HELPY]] Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
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[https://www.uniprot.org/uniprot/FUR_HELPY FUR_HELPY] Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fur, the ferric uptake regulator, is a transcription factor that controls iron metabolism in bacteria. Binding of ferrous iron to Fur triggers a conformational change that activates the protein for binding to specific DNA sequences named Fur boxes. In Helicobacter pylori, HpFur is involved in acid response and is important for gastric colonization in model animals. Here we present the crystal structure of a functionally active HpFur mutant (HpFur2M; C78S-C150S) bound to zinc. Although its fold is similar to that of other Fur and Fur-like proteins, the crystal structure of HpFur reveals a unique structured N-terminal extension and an unusual C-terminal helix. The structure also shows three metal binding sites: S1 the structural ZnS(4) site previously characterized biochemically in HpFur and the two zinc sites identified in other Fur proteins. Site-directed mutagenesis and spectroscopy analyses of purified wild-type HpFur and various mutants show that the two metal binding sites common to other Fur proteins can be also metallated by cobalt. DNA protection and circular dichroism experiments demonstrate that, while these two sites influence the affinity of HpFur for DNA, only one is absolutely required for DNA binding and could be responsible for the conformational changes of Fur upon metal binding while the other is a secondary site.
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The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites.,Dian C, Vitale S, Leonard GA, Bahlawane C, Fauquant C, Leduc D, Muller C, de Reuse H, Michaud-Soret I, Terradot L Mol Microbiol. 2011 Jan 5. doi: 10.1111/j.1365-2958.2010.07517.x. PMID:21208302<ref>PMID:21208302</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 2xig" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campylobacter pylori]]
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[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bahlawane, C]]
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[[Category: Bahlawane C]]
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[[Category: Dian, C]]
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[[Category: Dian C]]
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[[Category: Fauquant, F]]
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[[Category: Fauquant F]]
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[[Category: Leonard, G A]]
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[[Category: Leonard GA]]
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[[Category: Michaud-Soret, I]]
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[[Category: Michaud-Soret I]]
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[[Category: Muller, C]]
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[[Category: Muller C]]
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[[Category: Reuse, H de]]
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[[Category: Terradot L]]
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[[Category: Terradot, L]]
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[[Category: Vitale S]]
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[[Category: Vitale, S]]
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[[Category: De Reuse H]]
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[[Category: Homeostasis]]
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[[Category: Hpfur]]
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[[Category: Transcription]]
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Current revision

The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites

PDB ID 2xig

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