3ul3: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 3ul3~~ is ~~ON HOLD~~

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

== Structural highlights ==

<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='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'>[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>

== 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>

~~Authors~~: ~~Sharma, Ashwani, Sharma, Arvind, Dixit, Sameer, Sharma, Amit~~

==See Also==

*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]

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

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Plasmodium falciparum 3D7]]

[[Category: Dixit S]]

[[Category: Sharma A]]

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-'''Unreleased structure'''
-The entry 3ul3 is ON HOLD
+==Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery==
+<StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+</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>
-Authors: Sharma, Ashwani, Sharma, Arvind, Dixit, Sameer, Sharma, Amit
+==See Also==
+*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
-Description: Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Plasmodium falciparum 3D7]]
+[[Category: Dixit S]]
+[[Category: Sharma A]]