3ul3
From Proteopedia
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==Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery== | ==Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery== | ||
| - | <StructureSection load='3ul3' size='340' side='right' caption='[[3ul3]], [[Resolution|resolution]] 2.91Å' scene=''> | + | <StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ul3]] is a 2 chain structure with sequence from [ | + | <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> |
| - | </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]] 2.905Å</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=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> | ||
| + | == Function == | ||
| + | [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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| + | ==See Also== | ||
| + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: | + | [[Category: Dixit S]] |
| - | [[Category: | + | [[Category: Sharma A]] |
| - | + | ||
| - | + | ||
Current revision
Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery
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