1okt: Difference between revisions
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==X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum== | ==X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum== | ||
<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 [ | <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=' | </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=' | <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'>[ | <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_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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</div> | </div> | ||
<div class="pdbe-citations 1okt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1okt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
[[Category: | [[Category: Becker A]] | ||
[[Category: Becker K]] | |||
[[Category: Fritz-Wolf K]] | |||
[[Category: Harwaldt P]] | |||
[[Category: Kabsch W]] | |||
[[Category: Rahlfs s]] | |||
[[Category: Schirmer RH]] | |||
Latest revision as of 12:01, 9 May 2024
X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparumX-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum
Structural highlights
FunctionGST_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 PubMedGSTs 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 AlsoReferences
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