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1prx

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(New page: 200px<br /> <applet load="1prx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prx, resolution 2.0&Aring;" /> '''HORF6 A NOVEL HUMAN ...)
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[[Image:1prx.gif|left|200px]]<br />
 
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<applet load="1prx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1prx, resolution 2.0&Aring;" />
 
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''<br />
 
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==Overview==
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==HORF6 A NOVEL HUMAN PEROXIDASE ENZYME==
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Hydrogen peroxide (H2O2) has been implicated recently as an intracellular, messenger that affects cellular processes including protein, phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of, H2O2 by reducing it in the presence of an appropriate electron donor. The, crystal structure of a human Prx enzyme, hORF6, reveals that the protein, contains two discrete domains and forms a dimer. The N-terminal domain has, a thioredoxin fold and the C-terminal domain is used for dimerization. The, active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in, the crystal, is located at the bottom of a relatively narrow pocket. The, positively charged environment surrounding Cys 47 accounts for the, peroxidase activity of the enzyme, which contains no redox cofactors.
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<StructureSection load='1prx' size='340' side='right'caption='[[1prx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1prx]] is a 2 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=1PRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRX FirstGlance]. <br>
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1PRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA].
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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&#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=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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==Reference==
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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=1prx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prx OCA], [https://pdbe.org/1prx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prx RCSB], [https://www.ebi.ac.uk/pdbsum/1prx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prx ProSAT]</span></td></tr>
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Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9587003 9587003]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
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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/pr/1prx_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=1prx ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Choi, H.J.]]
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[[Category: Choi H-J]]
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[[Category: Kang, S.W.]]
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[[Category: Kang SW]]
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[[Category: Rhee, S.G.]]
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[[Category: Rhee SG]]
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[[Category: Ryu, S.E.]]
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[[Category: Ryu S-E]]
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[[Category: Yang, C.H.]]
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[[Category: Yang C-H]]
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[[Category: antioxidant]]
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[[Category: cellular signaling]]
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[[Category: horf6]]
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[[Category: hydrogen peroxide]]
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[[Category: peroxiredoxin]]
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[[Category: redox regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:46:34 2007''
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Current revision

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

PDB ID 1prx

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