2fe3
From Proteopedia
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| - | [[ | + | ==The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch== |
| + | <StructureSection load='2fe3' size='340' side='right' caption='[[2fe3]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2fe3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FE3 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fe3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fe3 RCSB], [http://www.ebi.ac.uk/pdbsum/2fe3 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == 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/fe/2fe3_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to H2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators. | ||
| - | + | Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis.,Traore DA, El Ghazouani A, Ilango S, Dupuy J, Jacquamet L, Ferrer JL, Caux-Thang C, Duarte V, Latour JM Mol Microbiol. 2006 Sep;61(5):1211-9. PMID:16925555<ref>PMID:16925555</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Traore, D A.K.]] | [[Category: Traore, D A.K.]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Oxidative stress regulator]] | [[Category: Oxidative stress regulator]] | ||
Revision as of 23:50, 29 September 2014
The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch
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