3ul3 | pdb_00003ul3

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

spinqualitylabelsall models 3ul3, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ul3 is a 2 chain structure with sequence from Plaf7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: MAL13P1.225, trx2 (PLAF7) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin

Proteopedia Page Contributors and Editors (what is this?)

OCA