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.
|Original language||English (US)|
|Number of pages||8|
|State||Published - Jan 14 2009|
Bibliographical noteFunding Information:
We acknowledge help from Hélène Déméné, Karine De Guillen, and Martin Cohen-Gonsaud for the recording of NMR and UV-CD spectra. We thank D. Svergun and his colleagues for assistance with SAXS data recording and analysis at the X33 beamline at EMBL/DESY, Hamburg. The authors thank Sergio Angel for providing the pQE-Rop2B plasmid. We acknowledge support from European Community—Research Infrastructure Action under the FP6 (RII3/CT/2004/5060008) for access to EMBL/DESY, Hamburg. We thank the ESRF staff for their help in recording diffraction data on beamlines ID14 and ID29. This work was supported by ANR-06-MIME-024-01.
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology