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[[Image:1m0u.jpg|left|200px]]<br /><applet load="1m0u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m0u, resolution 1.75&Aring;" />
'''Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione'''<br />


==Overview==
==Crystal Structure of the Drosophila Glutathione S-transferase-2 in Complex with Glutathione==
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.
<StructureSection load='1m0u' size='340' side='right'caption='[[1m0u]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== 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/m0/1m0u_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=1m0u ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1M0U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GSW:'>GSW</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0U OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12547198 12547198]
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Glutathione transferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Agianian B]]
[[Category: Agianian, B.]]
[[Category: Bullard B]]
[[Category: Bullard, B.]]
[[Category: Gros P]]
[[Category: Gros, P.]]
[[Category: Leonard K]]
[[Category: Leonard, K.]]
[[Category: Schouten A]]
[[Category: Schouten, A.]]
[[Category: Tucker PA]]
[[Category: Tucker, P A.]]
[[Category: GSW]]
[[Category: SO4]]
[[Category: flight muscle protein]]
[[Category: gst]]
[[Category: sigma]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:18 2008''

Latest revision as of 10:38, 14 February 2024

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

Structural highlights

1m0u is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Agianian B, Tucker PA, Schouten A, Leonard K, Bullard B, Gros P. Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. J Mol Biol. 2003 Feb 7;326(1):151-65. PMID:12547198
  2. ↑ Beall C, Fyrberg C, Song S, Fyrberg E. Isolation of a Drosophila gene encoding glutathione S-transferase. Biochem Genet. 1992 Oct;30(9-10):515-27. PMID:1445191 doi:10.1007/BF01037590
  3. ↑ Saisawang C, Wongsantichon J, Ketterman AJ. A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster. Biochem J. 2012 Feb 15;442(1):181-90. doi: 10.1042/BJ20111747. PMID:22082028 doi:http://dx.doi.org/10.1042/BJ20111747

1m0u, resolution 1.75Å

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