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| | <StructureSection load='2rgv' size='340' side='right'caption='[[2rgv]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='2rgv' size='340' side='right'caption='[[2rgv]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rgv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RGV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rgv]] 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=2RGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RGV 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]] 2.05Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fe3|2fe3]]</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=2rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgv OCA], [https://pdbe.org/2rgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rgv RCSB], [https://www.ebi.ac.uk/pdbsum/2rgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgv ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgv OCA], [http://pdbe.org/2rgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rgv RCSB], [http://www.ebi.ac.uk/pdbsum/2rgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgv ProSAT]</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]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgv_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgv_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Traore, D A.K]] | + | [[Category: Traore DAK]] |
| - | [[Category: 2-oxo-histidine]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Dna-binding]]
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| - | [[Category: Manganese]]
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| - | [[Category: Oxidation]]
| + | |
| - | [[Category: Perr-ox]]
| + | |
| - | [[Category: Repressor]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulation]]
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| - | [[Category: Zinc]]
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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, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe(2+) (PerR-Zn-Fe) or Mn(2+) (PerR-Zn-Mn). Though most of the peroxide sensors use cysteines to detect H(2)O(2), it has been shown that reaction of PerR-Zn-Fe with H(2)O(2) leads to the oxidation of one histidine residue. Oxidation of PerR leads to the incorporation of one oxygen atom into His37 or His91. This study presents the crystal structure of the oxidized PerR protein (PerR-Zn-ox), which clearly shows a 2-oxo-histidine residue in position 37. Formation of 2-oxo-histidine is demonstrated and quantified by HPLC-MS/MS. EPR experiments indicate that PerR-Zn-H37ox retains a significant affinity for the regulatory metal, whereas PerR-Zn-H91ox shows a considerably reduced affinity for the metal ion. In spite of these major differences in terms of metal binding affinity, oxidation of His37 and/or His91 in PerR prevents DNA binding.
Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein.,Traore DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, Duarte V, Latour JM Nat Chem Biol. 2009 Jan;5(1):53-9. Epub 2008 Dec 14. PMID:19079268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Traore DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, Duarte V, Latour JM. Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. Nat Chem Biol. 2009 Jan;5(1):53-9. Epub 2008 Dec 14. PMID:19079268 doi:10.1038/nchembio.133
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