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New page: left|200px<br /> <applet load="4gr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="4gr1, resolution 2.4Å" /> '''THE BINDING OF THE R...
 
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[[Image:4gr1.gif|left|200px]]<br />
<applet load="4gr1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="4gr1, resolution 2.4&Aring;" />
'''THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE'''<br />


==Overview==
==THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE==
The retro-analogue of glutathione disulfide was bound to the GSSG binding, site of crystalline glutathione reductase. The binding mode revealed why, the analogue is a very poor substrate in enzyme catalysis. The observed, binding mode difference between natural substrate and retro-analogue is, explained.
<StructureSection load='4gr1' size='340' side='right'caption='[[4gr1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gr1]] 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=4GR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GR1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RGS:4N-MALONYL-CYSTEINYL-2,4-DIAMINOBUTYRATE+DISULFIDE'>RGS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gr1 OCA], [https://pdbe.org/4gr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4gr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gr1 ProSAT]</span></td></tr>
</table>
== 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/gr/4gr1_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=4gr1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.


==Disease==
The binding of the retro-analogue of glutathione disulfide to glutathione reductase.,Janes W, Schulz GE J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009<ref>PMID:2355009</ref>
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]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
4GR1 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 RGS 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=4GR1 OCA].
</div>
<div class="pdbe-citations 4gr1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The binding of the retro-analogue of glutathione disulfide to glutathione reductase., Janes W, Schulz GE, J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2355009 2355009]
*[[Glutathione Reductase|Glutathione Reductase]]
[[Category: Glutathione-disulfide reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Janes, W.]]
[[Category: Janes W]]
[[Category: Schulz, G.E.]]
[[Category: Schulz GE]]
[[Category: FAD]]
[[Category: PO4]]
[[Category: RGS]]
[[Category: oxidoreductase (flavoenzyme)]]
 
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Latest revision as of 06:33, 17 October 2024

THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE

4gr1, resolution 2.40Å

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