3ul3: Difference between revisions

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New page: '''Unreleased structure''' The entry 3ul3 is ON HOLD Authors: Sharma, Ashwani, Sharma, Arvind, Dixit, Sameer, Sharma, Amit Description: Structural insights into thioredoxin-2: a compon...
 
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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]]

Latest revision as of 11:38, 20 March 2024

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

Structural highlights

3ul3 is a 2 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.905Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][1] [2] [3] [4]

See Also

References

  1. ↑ Nickel C, Rahlfs S, Deponte M, Koncarevic S, Becker K. Thioredoxin networks in the malarial parasite Plasmodium falciparum. Antioxid Redox Signal. 2006 Jul-Aug;8(7-8):1227-39. doi: 10.1089/ars.2006.8.1227. PMID:16910770 doi:http://dx.doi.org/10.1089/ars.2006.8.1227
  2. ↑ de Koning-Ward TF, Gilson PR, Boddey JA, Rug M, Smith BJ, Papenfuss AT, Sanders PR, Lundie RJ, Maier AG, Cowman AF, Crabb BS. A newly discovered protein export machine in malaria parasites. Nature. 2009 Jun 18;459(7249):945-9. doi: 10.1038/nature08104. PMID:19536257 doi:http://dx.doi.org/10.1038/nature08104
  3. ↑ Sharma A, Sharma A, Dixit S, Sharma A. Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery. Sci Rep. 2011;1:179. doi: 10.1038/srep00179. Epub 2011 Dec 1. PMID:22355694 doi:http://dx.doi.org/10.1038/srep00179
  4. ↑ de Koning-Ward TF, Gilson PR, Boddey JA, Rug M, Smith BJ, Papenfuss AT, Sanders PR, Lundie RJ, Maier AG, Cowman AF, Crabb BS. A newly discovered protein export machine in malaria parasites. Nature. 2009 Jun 18;459(7249):945-9. doi: 10.1038/nature08104. PMID:19536257 doi:http://dx.doi.org/10.1038/nature08104

3ul3, resolution 2.91Å

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