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[[Image:5gst.gif|left|200px]]
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{{STRUCTURE_5gst|  PDB=5gst  |  SCENE=  }}
'''REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE'''


==REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE==
<StructureSection load='5gst' size='340' side='right'caption='[[5gst]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gst]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GST 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDN:GLUTATHIONE+S-(2,4+DINITROBENZENE)'>GDN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5gst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gst OCA], [https://pdbe.org/5gst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gst RCSB], [https://www.ebi.ac.uk/pdbsum/5gst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gst ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
== 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/gs/5gst_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=5gst ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.


==Overview==
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.,Ji X, Armstrong RN, Gilliland GL Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:8241147<ref>PMID:8241147</ref>
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
5GST is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GST OCA].
</div>
<div class="pdbe-citations 5gst" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase., Ji X, Armstrong RN, Gilliland GL, Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8241147 8241147]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
[[Category: Glutathione transferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
[[Category: Single protein]]
[[Category: Armstrong RN]]
[[Category: Armstrong, R N.]]
[[Category: Gilliland GL]]
[[Category: Gilliland, G L.]]
[[Category: Ji X]]
[[Category: Ji, X.]]
[[Category: Glutathione transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:34:52 2008''

Latest revision as of 13:11, 30 August 2023

REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE

5gst, resolution 2.00Å

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