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| | <StructureSection load='2f8f' size='340' side='right'caption='[[2f8f]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2f8f' size='340' side='right'caption='[[2f8f]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f8f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F8F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f8f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F8F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='activity'><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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8f OCA], [http://pdbe.org/2f8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f8f RCSB], [http://www.ebi.ac.uk/pdbsum/2f8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8f ProSAT]</span></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=2f8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f8f OCA], [https://pdbe.org/2f8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f8f RCSB], [https://www.ebi.ac.uk/pdbsum/2f8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f8f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GST28_SCHBO GST28_SCHBO]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | + | [https://www.uniprot.org/uniprot/GST28_SCHBO GST28_SCHBO] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blood fluke]] | |
| - | [[Category: Glutathione transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Angelucci, F]] | + | [[Category: Schistosoma haematobium]] |
| - | [[Category: Baiocco, P]] | + | [[Category: Angelucci F]] |
| - | [[Category: Bellelli, A]] | + | [[Category: Baiocco P]] |
| - | [[Category: Brunori, M]] | + | [[Category: Bellelli A]] |
| - | [[Category: Gourlay, L J]] | + | [[Category: Brunori M]] |
| - | [[Category: Miele, A E]] | + | [[Category: Gourlay LJ]] |
| - | [[Category: Homodimer]]
| + | [[Category: Miele AE]] |
| - | [[Category: Protein_gtt complex]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
GST28_SCHBO Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
During turnover, the catalytic tyrosine residue (Tyr10) of the sigma class Schistosoma haematobium wild-type glutathione-S-transferase is expected to switch alternately in and out of the reduced glutathione-binding site (G-site). The Tyrout10 conformer forms a pi-cation interaction with the guanidinium group of Arg21. As in other similar glutathione-S-transferases, the catalytic Tyr has a low pKa of 7.2. In order to investigate the catalytic role of Tyr10, and the structural and functional roles of Arg21, we carried out structural studies on two Arg21 mutants (R21L and R21Q) and a Tyr10 mutant, Y10F. Our crystallographic data for the two Arg21 mutants indicate that only the Tyrout10 conformation is populated, thereby excluding a role of Arg21 in the stabilisation of the out conformation. However, Arg21 was confirmed to be catalytically important and essential for the low pKa of Tyr10. Upon comparison with structural data generated for reduced glutathione-bound and inhibitor-bound wild-type enzymes, it was observed that the orientations of Tyr10 and Arg35 are concerted and that, upon ligand binding, minor rearrangements occur within conserved residues in the active site loop. These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain.
Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography.,Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A. Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography. J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141 doi:10.1016/j.jmb.2006.05.040
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