1eem

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[[Image:1eem.gif|left|200px]]<br /><applet load="1eem" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eem, resolution 2.00&Aring;" />
 
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'''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''<br />
 
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==Overview==
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==GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS==
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<StructureSection load='1eem' size='340' side='right'caption='[[1eem]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eem]] 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=1EEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEM 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]] 2&#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=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1eem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eem OCA], [https://pdbe.org/1eem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eem RCSB], [https://www.ebi.ac.uk/pdbsum/1eem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eem ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTO1_HUMAN GSTO1_HUMAN] Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.<ref>PMID:10783391</ref> <ref>PMID:11511179</ref> <ref>PMID:17226937</ref> <ref>PMID:18028863</ref> <ref>PMID:21106529</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/1eem_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eem ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.
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==About this Structure==
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Identification, characterization, and crystal structure of the Omega class glutathione transferases.,Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J J Biol Chem. 2000 Aug 11;275(32):24798-806. PMID:10783391<ref>PMID:10783391</ref>
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1EEM 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEM OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Identification, characterization, and crystal structure of the Omega class glutathione transferases., Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J, J Biol Chem. 2000 Aug 11;275(32):24798-806. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10783391 10783391]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1eem" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Board, P.]]
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[[Category: Chelvanayagam, G.]]
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[[Category: Chrunyk, B A.]]
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[[Category: Coggan, M.]]
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[[Category: Danley, D E.]]
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[[Category: Easteal, S.]]
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[[Category: Gabel, C A.]]
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[[Category: Geoghegan, K F.]]
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[[Category: Griffor, M C.]]
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[[Category: Hoth, L R.]]
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[[Category: Jermiin, L S.]]
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[[Category: Kamath, A V.]]
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[[Category: Pandit, J.]]
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[[Category: Perregaux, D E.]]
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[[Category: Rosner, M H.]]
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[[Category: Schulte, G K.]]
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[[Category: GSH]]
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[[Category: SO4]]
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[[Category: glutathione conjugating]]
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[[Category: gst]]
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[[Category: putative oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:54 2008''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Board P]]
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[[Category: Chelvanayagam G]]
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[[Category: Chrunyk BA]]
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[[Category: Coggan M]]
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[[Category: Danley DE]]
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[[Category: Easteal S]]
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[[Category: Gabel CA]]
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[[Category: Geoghegan KF]]
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[[Category: Griffor MC]]
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[[Category: Hoth LR]]
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[[Category: Jermiin LS]]
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[[Category: Kamath AV]]
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[[Category: Pandit J]]
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[[Category: Perregaux DE]]
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[[Category: Rosner MH]]
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[[Category: Schulte GK]]

Current revision

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

PDB ID 1eem

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