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3ul3

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Current revision (08:38, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
<StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ul3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UL3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ul3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UL3 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAL13P1.225, trx2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.905&#8491;</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=3ul3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ul3 OCA], [https://pdbe.org/3ul3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ul3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ul3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ul3 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=3ul3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ul3 OCA], [https://pdbe.org/3ul3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ul3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ul3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ul3 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/THIO2_PLAF7 THIO2_PLAF7] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:16910770, PubMed:22355694). As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells (PubMed:19536257). May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function (PubMed:19536257).[UniProtKB:A0A509AQW5]<ref>PMID:16910770</ref> <ref>PMID:19536257</ref> <ref>PMID:22355694</ref> <ref>PMID:19536257</ref>
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Thioredoxins are vital components of Plasmodium proteome and act as both reducing agents and protein disulfide reductases. The malaria parasite P. falciparum thioredoxin-2 (PfTrx-2) is part of the multi-protein complex embedded within the parasite parasitophorous vacuolar membrane (PVM) which purportedly directs protein secretion. We have characterized structural and enzymatic features of PfTrx-2, and we show that PfTrx-2 adopts a canonical thioredoxin fold but with significant structural differences in its N-terminus. Our confocal localization data suggest distinct PVM residency of PfTrx-2. Based on the crystal structure of PfTrx-2, we screened and tested small molecule drug-like libraries for compounds which target unique structural features of PfTrx-2. Disruption of PfTrx-2 interactions using specific inhibitors may result in a dysfunctional parasite translocon that is rendered unable to secrete pathogenic proteins into hosts. This approach therefore offers a new focus for anti-malarial drug development.
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Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery.,Sharma A, Sharma A, Dixit S, Sharma A Sci Rep. 2011;1:179. doi: 10.1038/srep00179. Epub 2011 Dec 1. PMID:22355694<ref>PMID:22355694</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ul3" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Plaf7]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Dixit, S]]
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[[Category: Dixit S]]
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[[Category: Sharma, A]]
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[[Category: Sharma A]]
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[[Category: Oxidoreductase]]
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[[Category: Ptex]]
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[[Category: Thioredoxin]]
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Current revision

Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery

PDB ID 3ul3

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