1eem

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[[Image:1eem.gif|left|200px]]
 
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{{Structure
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==GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS==
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|PDB= 1eem |SIZE=350|CAPTION= <scene name='initialview01'>1eem</scene>, resolution 2.00&Aring;
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<StructureSection load='1eem' size='340' side='right'caption='[[1eem]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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}}
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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 ==
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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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'''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''
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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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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 1eem" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1EEM 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=1EEM OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10783391 10783391]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Board, P.]]
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[[Category: Board P]]
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[[Category: Chelvanayagam, G.]]
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[[Category: Chelvanayagam G]]
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[[Category: Chrunyk, B A.]]
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[[Category: Chrunyk BA]]
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[[Category: Coggan, M.]]
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[[Category: Coggan M]]
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[[Category: Danley, D E.]]
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[[Category: Danley DE]]
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[[Category: Easteal, S.]]
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[[Category: Easteal S]]
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[[Category: Gabel, C A.]]
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[[Category: Gabel CA]]
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[[Category: Geoghegan, K F.]]
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[[Category: Geoghegan KF]]
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[[Category: Griffor, M C.]]
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[[Category: Griffor MC]]
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[[Category: Hoth, L R.]]
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[[Category: Hoth LR]]
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[[Category: Jermiin, L S.]]
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[[Category: Jermiin LS]]
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[[Category: Kamath, A V.]]
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[[Category: Kamath AV]]
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[[Category: Pandit, J.]]
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[[Category: Pandit J]]
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[[Category: Perregaux, D E.]]
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[[Category: Perregaux DE]]
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[[Category: Rosner, M H.]]
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[[Category: Rosner MH]]
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[[Category: Schulte, G K.]]
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[[Category: Schulte GK]]
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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 Mar 20 10:54:34 2008''
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Current revision

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

PDB ID 1eem

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