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| | <StructureSection load='1okt' size='340' side='right'caption='[[1okt]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1okt' size='340' side='right'caption='[[1okt]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1okt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1okt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OKT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.9Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://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=FMT:FORMIC+ACID'>FMT</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=1okt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okt OCA], [https://pdbe.org/1okt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okt RCSB], [https://www.ebi.ac.uk/pdbsum/1okt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okt 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=1okt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okt OCA], [https://pdbe.org/1okt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1okt RCSB], [https://www.ebi.ac.uk/pdbsum/1okt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1okt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GST_PLAFA GST_PLAFA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).<ref>PMID:12108547</ref> <ref>PMID:12387854</ref> <ref>PMID:16385005</ref>
| + | [https://www.uniprot.org/uniprot/GST_PLAF7 GST_PLAF7] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).<ref>PMID:12108547</ref> <ref>PMID:12387854</ref> <ref>PMID:16385005</ref> |
| | == 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: Glutathione transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Plafa]] | |
| - | [[Category: Becker, A]] | |
| - | [[Category: Becker, K]] | |
| - | [[Category: Fritz-Wolf, K]] | |
| - | [[Category: Harwaldt, P]] | |
| - | [[Category: Kabsch, W]] | |
| - | [[Category: Rahlfs, s]] | |
| - | [[Category: Schirmer, R H]] | |
| - | [[Category: Gst]] | |
| | [[Category: Plasmodium falciparum]] | | [[Category: Plasmodium falciparum]] |
| - | [[Category: Transferase]] | + | [[Category: Becker A]] |
| | + | [[Category: Becker K]] |
| | + | [[Category: Fritz-Wolf K]] |
| | + | [[Category: Harwaldt P]] |
| | + | [[Category: Kabsch W]] |
| | + | [[Category: Rahlfs s]] |
| | + | [[Category: Schirmer RH]] |
| Structural highlights
Function
GST_PLAF7 Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).[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.
Publication Abstract from PubMed
GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is highly abundant in the parasite, its activity was found to be increased in chloroquine-resistant cells, and it has been shown to act as a ligandin for parasitotoxic hemin. Thus, the enzyme represents a promising target for antimalarial drug development. We now have solved the crystal structure of PfGST at a resolution of 1.9 A. The homodimeric protein of 26 kDa per subunit represents a GST form that cannot be assigned to any of the known GST classes. In comparison to other GSTs, and, in particular, to the human isoforms, PfGST possesses a shorter C-terminal section resulting in a more solvent-accessible binding site for the hydrophobic and amphiphilic substrates. The structure furthermore reveals features in this region that could be exploited for the design of specific PfGST inhibitors.
X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.,Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13821-6. Epub 2003 Nov 17. PMID:14623980[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Harwaldt P, Rahlfs S, Becker K. Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target. Biol Chem. 2002 May;383(5):821-30. PMID:12108547 doi:http://dx.doi.org/10.1515/BC.2002.086
- ↑ Liebau E, Bergmann B, Campbell AM, Teesdale-Spittle P, Brophy PM, Luersen K, Walter RD. The glutathione S-transferase from Plasmodium falciparum. Mol Biochem Parasitol. 2002 Sep-Oct;124(1-2):85-90. PMID:12387854
- ↑ Hiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K. Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition. Protein Sci. 2006 Feb;15(2):281-9. Epub 2005 Dec 29. PMID:16385005 doi:10.1110/ps.051891106
- ↑ Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K. X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum. Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13821-6. Epub 2003 Nov 17. PMID:14623980 doi:10.1073/pnas.2333763100
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