2rgv

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{{Seed}}
 
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[[Image:2rgv.png|left|200px]]
 
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==The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation==
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The line below this paragraph, containing "STRUCTURE_2rgv", creates the "Structure Box" on the page.
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<StructureSection load='2rgv' size='340' side='right'caption='[[2rgv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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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]] 2.05&#8491;</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=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2rgv| PDB=2rgv | SCENE= }}
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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=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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2rgv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation===
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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<ref>PMID:19079268</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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The line below this paragraph, {{ABSTRACT_PUBMED_19079268}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2rgv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19079268 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19079268}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2RGV is a [[Single protein]] structure of 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=2RGV OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/19079268 19079268]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: Traore DAK]]
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[[Category: 2-oxo-histidine]]
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[[Category: Cytoplasm]]
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[[Category: Dna binding protein]]
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[[Category: Dna-binding]]
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[[Category: Manganese]]
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[[Category: Oxidation]]
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[[Category: Perr-ox]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 20:21:45 2009''
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Current revision

The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation

PDB ID 2rgv

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