1gsn

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(New page: 200px<br /> <applet load="1gsn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsn, resolution 1.7&Aring;" /> '''HUMAN GLUTATHIONE RE...)
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[[Image:1gsn.gif|left|200px]]<br />
 
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<applet load="1gsn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gsn, resolution 1.7&Aring;" />
 
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'''HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE'''<br />
 
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==Overview==
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==HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE==
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Nitric oxide (NO) is a pluripotent regulatory molecule, yet the molecular, mechanisms by which it exerts its effects are largely unknown. Few, physiologic target molecules of NO have been identified, and even for, these, the modifications caused by NO remain uncharacterized. Human, glutathione reductase (hGR), a central enzyme of cellular antioxidant, defense, is inhibited by S-nitrosoglutathione (GSNO) and by, diglutathionyl-dinitroso-iron (DNIC-[GSH]2), two in vivo transport forms, of NO. Here, crystal structures of hGR inactivated by GSNO and DNIC-[GSH]2, at 1.7 A resolution provide the first picture of enzyme inactivation by, NO-carriers: in GSNO-modified hGR, the active site residue Cys 63 is, oxidized to an unusually stable cysteine sulfenic acid (R-SOH), whereas, modification with DNIC-[GSH]2 oxidizes Cys 63 to a cysteine sulfinic acid, (R-SO2H). Our results illustrate that various forms of NO can mediate, distinct chemistry, and that sulfhydryl oxidation must be considered as a, major mechanism of NO action.
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<StructureSection load='1gsn' size='340' side='right'caption='[[1gsn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gsn]] 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=1GSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSN FirstGlance]. <br>
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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]] 1.7&#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>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=1gsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsn OCA], [https://pdbe.org/1gsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsn RCSB], [https://www.ebi.ac.uk/pdbsum/1gsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.
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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/gs/1gsn_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=1gsn 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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Nitric oxide (NO) is a pluripotent regulatory molecule, yet the molecular mechanisms by which it exerts its effects are largely unknown. Few physiologic target molecules of NO have been identified, and even for these, the modifications caused by NO remain uncharacterized. Human glutathione reductase (hGR), a central enzyme of cellular antioxidant defense, is inhibited by S-nitrosoglutathione (GSNO) and by diglutathionyl-dinitroso-iron (DNIC-[GSH]2), two in vivo transport forms of NO. Here, crystal structures of hGR inactivated by GSNO and DNIC-[GSH]2 at 1.7 A resolution provide the first picture of enzyme inactivation by NO-carriers: in GSNO-modified hGR, the active site residue Cys 63 is oxidized to an unusually stable cysteine sulfenic acid (R-SOH), whereas modification with DNIC-[GSH]2 oxidizes Cys 63 to a cysteine sulfinic acid (R-SO2H). Our results illustrate that various forms of NO can mediate distinct chemistry, and that sulfhydryl oxidation must be considered as a major mechanism of NO action.
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==Disease==
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Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers.,Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:9546215<ref>PMID:9546215</ref>
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Known disease associated with this structure: Hemolytic anemia due to glutathione reductase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138300 138300]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1GSN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4, FAD and GTT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSN OCA].
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</div>
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<div class="pdbe-citations 1gsn" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers., Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA, Nat Struct Biol. 1998 Apr;5(4):267-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546215 9546215]
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*[[Glutathione Reductase|Glutathione Reductase]]
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[[Category: Glutathione-disulfide reductase]]
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== References ==
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<references/>
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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: Becker, K.]]
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[[Category: Becker K]]
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[[Category: Karplus, P.A.]]
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[[Category: Karplus PA]]
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[[Category: Keese, M.]]
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[[Category: Keese M]]
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[[Category: Savvides, S.N.]]
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[[Category: Savvides SN]]
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[[Category: Schirmer, R.H.]]
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[[Category: Schirmer RH]]
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[[Category: FAD]]
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[[Category: GTT]]
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[[Category: PO4]]
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[[Category: nitric oxide]]
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[[Category: oxidoreductase]]
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[[Category: sulfenic acid]]
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[[Category: sulfhydryl oxidation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:08:47 2007''
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HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE

PDB ID 1gsn

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