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| | ==Crystal structure of PerR-Zn-Mn== | | ==Crystal structure of PerR-Zn-Mn== |
| - | <StructureSection load='3f8n' size='340' side='right' caption='[[3f8n]], [[Resolution|resolution]] 3.15Å' scene=''> | + | <StructureSection load='3f8n' size='340' side='right'caption='[[3f8n]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3f8n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3f8n]] 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=3F8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F8N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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]] 3.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fe3|2fe3]], [[2rgv|2rgv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">perR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=3f8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f8n OCA], [https://pdbe.org/3f8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f8n RCSB], [https://www.ebi.ac.uk/pdbsum/3f8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f8n ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f8n OCA], [http://pdbe.org/3f8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f8n RCSB], [http://www.ebi.ac.uk/pdbsum/3f8n PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/3f8n_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/3f8n_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Duarte, V]] | + | [[Category: Large Structures]] |
| - | [[Category: Ferrer, J L]] | + | [[Category: Duarte V]] |
| - | [[Category: Jacquamet, L]] | + | [[Category: Ferrer J-L]] |
| - | [[Category: Latour, J M]] | + | [[Category: Jacquamet L]] |
| - | [[Category: Traore, D A.K]] | + | [[Category: Latour J-M]] |
| - | [[Category: Dna binding protein]]
| + | [[Category: Traore DAK]] |
| - | [[Category: Dna-binding]]
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| - | [[Category: Helix-turn-helix]]
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| - | [[Category: Manganese]]
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| - | [[Category: Oxidation]]
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| - | [[Category: Repressor]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H(2)O(2). The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn(2+) ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta-coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding.,Jacquamet L, Traore DA, Ferrer JL, Proux O, Testemale D, Hazemann JL, Nazarenko E, El Ghazouani A, Caux-Thang C, Duarte V, Latour JM Mol Microbiol. 2009 Jul;73(1):20-31. Epub 2009 Jun 8. PMID:19508285[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacquamet L, Traore DA, Ferrer JL, Proux O, Testemale D, Hazemann JL, Nazarenko E, El Ghazouani A, Caux-Thang C, Duarte V, Latour JM. Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding. Mol Microbiol. 2009 Jul;73(1):20-31. Epub 2009 Jun 8. PMID:19508285 doi:10.1111/j.1365-2958.2009.06753.x
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