Download MendeleyRop2 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, S.T., Dubremetz, J.-F.(2009) Structure 17: 139
- PubMed: 19141290
- DOI: https://doi.org/10.1016/j.str.2008.11.005
- Primary Citation of Related Structures:
2W1Z - PubMed 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.
Organizational Affiliation:
Atelier de Bio- et Chimie Informatique Structurale, Centre de Biochimie Structurale, CNRS, UMR5048, Universités Montpellier 1 et 2, F34090 Montpellier, France. labesse@cbs.cnrs.fr
