4o32

Structural highlights

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

• Thioredoxin 3D structures

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