3mng

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{{Seed}}
 
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[[Image:3mng.png|left|200px]]
 
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==wild type human PrxV with DTT bound as a competitive inhibitor==
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The line below this paragraph, containing "STRUCTURE_3mng", creates the "Structure Box" on the page.
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<StructureSection load='3mng' size='340' side='right'caption='[[3mng]], [[Resolution|resolution]] 1.45&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'>[[3mng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MNG 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]] 1.45&#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=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_3mng| PDB=3mng | 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=3mng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mng OCA], [https://pdbe.org/3mng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mng RCSB], [https://www.ebi.ac.uk/pdbsum/3mng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mng ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRDX5_HUMAN PRDX5_HUMAN] Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.
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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/mn/3mng_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3mng 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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Peroxiredoxins (Prxs) are important peroxidases associated with both antioxidant protection and redox signaling. They use a conserved Cys residue to reduce peroxide substrates. The Prxs have a remarkably high catalytic efficiency that makes them a dominant player in cell-wide peroxide reduction, but the origins of their high activity have been mysterious. We present here a novel structure of human PrxV at 1.45 A resolution that has a dithiothreitol bound in the active site with its diol moiety mimicking the two oxygens of a peroxide substrate. This suggests diols and similar di-oxygen compounds as a novel class of competitive inhibitors for the Prxs. Common features of this and other structures containing peroxide, peroxide-mimicking ligands, or peroxide-mimicking water molecules reveal hydrogen bonding and steric factors that promote its high reactivity by creating an oxygen track along which the peroxide oxygens move as the reaction proceeds. Key insights include how the active-site microenvironment activates both the peroxidatic cysteine side chain and the peroxide substrate and how it is exquisitely well suited to stabilize the transition state of the in-line S(N)2 substitution reaction that is peroxidation.
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===wild type human PrxV with DTT bound as a competitive inhibitor===
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Structural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State Stabilization.,Hall A, Parsonage D, Poole LB, Karplus PA J Mol Biol. 2010 Sep 10;402(1):194-209. Epub 2010 Jul 17. PMID:20643143<ref>PMID:20643143</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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<div class="pdbe-citations 3mng" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20643143}}, adds the Publication Abstract to the page
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*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20643143 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20643143}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3MNG is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MNG OCA].
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==Reference==
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<ref group="xtra">PMID:20643143</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Peroxiredoxin]]
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[[Category: Large Structures]]
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[[Category: Hall, A.]]
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[[Category: Hall A]]
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[[Category: Karplus, P A.]]
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[[Category: Karplus PA]]
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[[Category: Dtt]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxidase]]
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[[Category: Peroxiredoxin]]
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[[Category: Prxv]]
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[[Category: Substrate analog]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:25:26 2010''
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Current revision

wild type human PrxV with DTT bound as a competitive inhibitor

PDB ID 3mng

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OCA

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