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1tu7

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{{STRUCTURE_1tu7| PDB=1tu7 | SCENE= }}
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==Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase==
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===Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase===
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<StructureSection load='1tu7' size='340' side='right' caption='[[1tu7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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{{ABSTRACT_PUBMED_15640152}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncvo Oncvo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TU7 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tu8|1tu8]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6282 ONCVO])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tu7 RCSB], [http://www.ebi.ac.uk/pdbsum/1tu7 PDBsum]</span></td></tr>
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<table>
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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/tu/1tu7_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/chain_selection.php?pdb_ID=2ata 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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Onchocerciasis is a debilitating parasitic disease caused by the filarial worm Onchocerca volvulus. Similar to other helminth parasites, O. volvulus is capable of evading the host's immune responses by a variety of defense mechanisms, including the detoxification activities of the glutathione S-transferases (GSTs). Additionally, in response to drug treatment, helminth GSTs are highly up-regulated, making them tempting targets both for chemotherapy and for vaccine development. We analyzed the three-dimensional x-ray structure of the major cytosolic GST from O. volvulus (Ov-GST2) in complex with its natural substrate glutathione and its competitive inhibitor S-hexylglutathione at 1.5 and 1.8 angstrom resolution, respectively. From the perspective of the biochemical classification, the Ov-GST2 seems to be related to pi-class GSTs. However, in comparison to other pi-class GSTs, in particular to the host's counterpart, the Ov-GST2 reveals significant and unusual differences in the sequence and overall structure. Major differences can be found in helix alpha-2, an important region for substrate recognition. Moreover, the binding site for the electrophilic co-substrate is spatially increased and more solvent-accessible. These structural alterations are responsible for different substrate specificities and will form the basis of parasite-specific structure-based drug design investigations.
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==Function==
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Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.,Perbandt M, Hoppner J, Betzel C, Walter RD, Liebau E J Biol Chem. 2005 Apr 1;280(13):12630-6. Epub 2005 Jan 7. PMID:15640152<ref>PMID:15640152</ref>
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[[http://www.uniprot.org/uniprot/GSTP_ONCVO GSTP_ONCVO]] Appears to play a central role in the parasite detoxification system.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[1tu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncvo Oncvo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU7 OCA].
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</div>
==See Also==
==See Also==
*[[Glutathione S-transferase|Glutathione S-transferase]]
*[[Glutathione S-transferase|Glutathione S-transferase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015640152</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Oncvo]]
[[Category: Oncvo]]
[[Category: Perbandt, M.]]
[[Category: Perbandt, M.]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 09:14, 3 October 2014

Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase

1tu7, resolution 1.50Å

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