ROP2 from Toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity

Structure
Gilles LabesseJean-François Dubremetz

Abstract

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.

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Citations

Nov 5, 2013·International Journal for Parasitology·Isabelle Coppens
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Mar 30, 2021·Veterinary Parasitology·Yakun WangXiaomin Zhao

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