Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Structural highlights
3fr6 is a 2 chain structure with sequence from Plasmodium falciparum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
GST_PLAF7 Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Harwaldt P, Rahlfs S, Becker K. Glutathione S-transferase of the malarial parasite Plasmodium falciparum: characterization of a potential drug target. Biol Chem. 2002 May;383(5):821-30. PMID:12108547 doi:http://dx.doi.org/10.1515/BC.2002.086
↑Liebau E, Bergmann B, Campbell AM, Teesdale-Spittle P, Brophy PM, Luersen K, Walter RD. The glutathione S-transferase from Plasmodium falciparum. Mol Biochem Parasitol. 2002 Sep-Oct;124(1-2):85-90. PMID:12387854
↑Hiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K. Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition. Protein Sci. 2006 Feb;15(2):281-9. Epub 2005 Dec 29. PMID:16385005 doi:10.1110/ps.051891106
