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1m0u

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[[Image:1m0u.jpg|left|200px]]
 
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==Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione==
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The line below this paragraph, containing "STRUCTURE_1m0u", creates the "Structure Box" on the page.
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<StructureSection load='1m0u' size='340' side='right'caption='[[1m0u]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1m0u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M0U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.75&#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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{{STRUCTURE_1m0u| PDB=1m0u | 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=1m0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0u OCA], [https://pdbe.org/1m0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m0u RCSB], [https://www.ebi.ac.uk/pdbsum/1m0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m0u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTS1_DROME GSTS1_DROME] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). May be involved in the detoxification of metabolites produced during cellular division and morphogenesis (PubMed:1445191, PubMed:12547198).<ref>PMID:12547198</ref> <ref>PMID:1445191</ref> <ref>PMID:22082028</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/m0/1m0u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1m0u ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione'''
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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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==Overview==
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<references/>
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Insect glutathione-S-transferases (GSTs) are grouped in three classes, I, II and recently III; class I (Delta class) enzymes together with class III members are implicated in conferring resistance to insecticides. Class II (Sigma class) GSTs, however, are poorly characterized and their exact biological function remains elusive. Drosophila glutathione S-transferase-2 (GST-2) (DmGSTS1-1) is a class II enzyme previously found associated specifically with the insect indirect flight muscle. It was recently shown that GST-2 exhibits considerable conjugation activity for 4-hydroxynonenal (4-HNE), a lipid peroxidation product, raising the possibility that it has a major anti-oxidant role in the flight muscle. Here, we report the crystal structure of GST-2 at 1.75A resolution. The GST-2 dimer shows the canonical GST fold with glutathione (GSH) ordered in only one of the two binding sites. While the GSH-binding mode is similar to other GST structures, a distinct orientation of helix alpha6 creates a novel electrophilic substrate-binding site (H-site) topography, largely flat and without a prominent hydrophobic-binding pocket, which characterizes the H-sites of other GSTs. The H-site displays directionality in the distribution of charged/polar and hydrophobic residues creating a binding surface that explains the selectivity for amphipolar peroxidation products, with the polar-binding region formed by residues Y208, Y153 and R145 and the hydrophobic-binding region by residues V57, A59, Y211 and the C-terminal V249. A structure-based model of 4-HNE binding is presented. The model suggest that residues Y208, R145 and possibly Y153 may be key residues involved in catalysis.
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__TOC__
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</StructureSection>
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==About this Structure==
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1M0U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0U OCA].
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==Reference==
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Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products., Agianian B, Tucker PA, Schouten A, Leonard K, Bullard B, Gros P, J Mol Biol. 2003 Feb 7;326(1):151-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12547198 12547198]
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Agianian B]]
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[[Category: Agianian, B.]]
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[[Category: Bullard B]]
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[[Category: Bullard, B.]]
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[[Category: Gros P]]
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[[Category: Gros, P.]]
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[[Category: Leonard K]]
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[[Category: Leonard, K.]]
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[[Category: Schouten A]]
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[[Category: Schouten, A.]]
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[[Category: Tucker PA]]
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[[Category: Tucker, P A.]]
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[[Category: Flight muscle protein]]
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[[Category: Gst]]
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[[Category: Sigma]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:29:39 2008''
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Current revision

Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione

PDB ID 1m0u

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