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[[Image:4gr1.gif|left|200px]]
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{{STRUCTURE_4gr1|  PDB=4gr1  |  SCENE=  }}
'''THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE'''


==THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE==
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
4GR1 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=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://www.ncbi.nlm.nih.gov/pubmed/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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:24:39 2008''

Latest revision as of 09:33, 17 October 2024

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

Structural highlights

4gr1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSHR_HUMAN Maintains high levels of reduced glutathione in the cytosol.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Janes W, Schulz GE. The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009

4gr1, resolution 2.40Å

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