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3q18

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[[Image:3q18.png|left|200px]]
 
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==Human Glutathione Transferase O2==
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The line below this paragraph, containing "STRUCTURE_3q18", creates the "Structure Box" on the page.
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<StructureSection load='3q18' size='340' side='right'caption='[[3q18]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3q18]] is a 2 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=3Q18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q18 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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{{STRUCTURE_3q18| PDB=3q18 | SCENE= }}
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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=3q18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q18 OCA], [https://pdbe.org/3q18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q18 RCSB], [https://www.ebi.ac.uk/pdbsum/3q18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q18 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTO2_HUMAN GSTO2_HUMAN] Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).<ref>PMID:15970797</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The reduction of dehydroascorbate (DHA) to ascorbic acid (AA) is a vital cellular function. The omega-class glutathione S-transferases (GSTs) catalyze several reductive reactions in cellular biochemistry, including DHA reduction. In humans, two isozymes (GSTO1-1 and GSTO2-2) with significant DHA reductase (DHAR) activity are found, sharing 64% sequence identity. While the activity of GSTO2-2 is higher, it is significantly more unstable in vitro. We report the first crystal structures of human GSTO2-2, stabilized through site-directed mutagenesis and determined at 1.9 A resolution in the presence and absence of glutathione (GSH). The structure of a human GSTO1-1 has been determined at 1.7 A resolution in complex with the reaction product AA, which unexpectedly binds in the G-site, where the glutamyl moiety of GSH binds. The structure suggests a similar mode of ascorbate binding in GSTO2-2. This is the first time that a non-GSH-based reaction product has been observed in the G-site of any GST. AA stacks against a conserved aromatic residue, F34 (equivalent to Y34 in GSTO2-2). Mutation of Y34 to alanine in GSTO2-2 eliminates DHAR activity. From these structures and other biochemical data, we propose a mechanism of substrate binding and catalysis of DHAR activity.
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===Human Glutathione Transferase O2===
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Structural Insights into the Dehydroascorbate Reductase Activity of Human Omega-Class Glutathione Transferases.,Zhou H, Brock J, Liu D, Board PG, Oakley AJ J Mol Biol. 2012 Apr 18. PMID:22522127<ref>PMID:22522127</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3q18" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22522127 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22522127}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3q18]] is a 2 chain structure with 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=3Q18 OCA].
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==Reference==
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<ref group="xtra">PMID:022522127</ref><references group="xtra"/>
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[[Category: Glutathione transferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Board, P G.]]
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[[Category: Large Structures]]
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[[Category: Oakley, A J.]]
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[[Category: Board PG]]
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[[Category: Zhou, H.]]
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[[Category: Oakley AJ]]
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[[Category: Dehydroascorbate reductase]]
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[[Category: Zhou H]]
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[[Category: Glutathione transferase]]
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[[Category: Gst]]
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[[Category: Reductase]]
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[[Category: Transferase]]
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Current revision

Human Glutathione Transferase O2

PDB ID 3q18

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