The ROP2 protein and its paralogs are important virulence factors secreted into the host cell by the parasite Toxoplasma gondii. Here we describe the crystal structure of a large and soluble domain of mature ROP2, representative of the ROP2-like protein family. This is a structure of a protein-kinase fold that is devoid of catalytic residues and does not bind ATP. Various structural extensions constitute a signature of this protein family and act to maintain the protein kinase in an open conformation. Our ROP2 structure rules out a previous structural model of attachment of ROP2-like proteins to the parasitophorous vacuole membrane. We propose an alternative mode of membrane attachment implicating basic and amphiphatic helices present in the flexible N terminus of ROP2.
ROP2 from Toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity.,Labesse G, Gelin M, Bessin Y, Lebrun M, Papoin J, Cerdan R, Arold ST, Dubremetz JF Structure. 2009 Jan 14;17(1):139-46. PMID:19141290[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Labesse G, Gelin M, Bessin Y, Lebrun M, Papoin J, Cerdan R, Arold ST, Dubremetz JF. ROP2 from Toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity. Structure. 2009 Jan 14;17(1):139-46. PMID:19141290 doi:10.1016/j.str.2008.11.005
