2fe3
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2fe3' size='340' side='right'caption='[[2fe3]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='2fe3' size='340' side='right'caption='[[2fe3]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2fe3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2fe3]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2FE3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.75Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2fe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fe3 OCA], [https://pdbe.org/2fe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fe3 RCSB], [https://www.ebi.ac.uk/pdbsum/2fe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fe3 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=2fe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fe3 OCA], [https://pdbe.org/2fe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fe3 RCSB], [https://www.ebi.ac.uk/pdbsum/2fe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fe3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PERR_BACSU PERR_BACSU] Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</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=2fe3 ConSurf]. | </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=2fe3 ConSurf]. | ||
<div style="clear:both"></div> | <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> | ||
| - | <div class="pdbe-citations 2fe3" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Traore | + | [[Category: Traore DAK]] |
| - | + | ||
| - | + | ||
Current revision
The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch
| |||||||||||
