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[[Image:1k4q.jpg|left|200px]]


{{Structure
==Human Glutathione Reductase Inactivated by Peroxynitrite==
|PDB= 1k4q |SIZE=350|CAPTION= <scene name='initialview01'>1k4q</scene>, resolution 1.9&Aring;
<StructureSection load='1k4q' size='340' side='right'caption='[[1k4q]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene>
<table><tr><td colspan='2'>[[1k4q]] 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=1K4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4Q FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4q OCA], [https://pdbe.org/1k4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4q RCSB], [https://www.ebi.ac.uk/pdbsum/1k4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4q ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4q OCA], [http://www.ebi.ac.uk/pdbsum/1k4q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4q RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/1k4q_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1k4q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As part of our studies on the nitric oxide-related pathology of cerebral malaria, we show that the antioxidative enzyme glutathione reductase (GR) is inactivated by peroxynitrite, with GR from the malarial parasite Plasmodium falciparum being more sensitive than human GR. The crystal structure of modified human GR at 1.9-A resolution provides the first picture of protein inactivation by peroxynitrite and reveals that this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site. The selective nitration explains the impairment of binding the peptide substrate and thus the nearly 1000-fold decrease in catalytic efficiency (k(cat)/K(m)) of glutathione reductase observed at physiologic pH. By oxidizing the catalytic dithiol to a disulfide, peroxynitrite itself can act as a substrate of unmodified and bisnitrated P. falciparum glutathione reductase.


'''Human Glutathione Reductase Inactivated by Peroxynitrite'''
Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite.,Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH J Biol Chem. 2002 Jan 25;277(4):2779-84. Epub 2001 Nov 8. PMID:11705998<ref>PMID:11705998</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k4q" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
As part of our studies on the nitric oxide-related pathology of cerebral malaria, we show that the antioxidative enzyme glutathione reductase (GR) is inactivated by peroxynitrite, with GR from the malarial parasite Plasmodium falciparum being more sensitive than human GR. The crystal structure of modified human GR at 1.9-A resolution provides the first picture of protein inactivation by peroxynitrite and reveals that this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site. The selective nitration explains the impairment of binding the peptide substrate and thus the nearly 1000-fold decrease in catalytic efficiency (k(cat)/K(m)) of glutathione reductase observed at physiologic pH. By oxidizing the catalytic dithiol to a disulfide, peroxynitrite itself can act as a substrate of unmodified and bisnitrated P. falciparum glutathione reductase.
*[[Glutathione Reductase|Glutathione Reductase]]
 
== References ==
==About this Structure==
<references/>
1K4Q is a [[Single protein]] structure of 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=1K4Q OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite., Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH, J Biol Chem. 2002 Jan 25;277(4):2779-84. Epub 2001 Nov 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11705998 11705998]
[[Category: Glutathione-disulfide reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arteel, G E.]]
[[Category: Arteel GE]]
[[Category: Becker, K.]]
[[Category: Becker K]]
[[Category: Boehme, C C.]]
[[Category: Boehme CC]]
[[Category: Karplus, P A.]]
[[Category: Karplus PA]]
[[Category: Savvides, S N.]]
[[Category: Savvides SN]]
[[Category: Scheiwein, M.]]
[[Category: Scheiwein M]]
[[Category: Schirmer, R H.]]
[[Category: Schirmer RH]]
[[Category: flavoenzyme]]
[[Category: nitrotyrosine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:27 2008''

Latest revision as of 22:05, 26 March 2025

Human Glutathione Reductase Inactivated by Peroxynitrite

1k4q, resolution 1.90Å

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