2W1Z

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

Summary for 2W1Z

• Entry DOI: 10.2210/pdb2w1z/pdb
• Descriptor: ROP2, SULFATE ION (3 entities in total)
• Functional Keywords: inactivity, protein-kinase, membrane-attachment, transferase
• Biological source: TOXOPLASMA GONDII
• Total number of polymer chains: 2
• Total formula weight: 85619.55

Authors

Labesse, G.,Gelin, M.,Bessin, Y.,Lebrun, M.,Arold, S.T.,Dubremetz, J.-F. (deposition date: 2008-10-21, release date: 2008-12-09, Last modification date: 2024-10-23)

Primary citation

Labesse, G.,Gelin, M.,Bessin, Y.,Lebrun, M.,Papoin, J.,Cerdan, R.,Arold, S.T.,Dubremetz, J.-F.
Rop2 from Toxoplasma Gondii: A Virulence Factor with a Protein-Kinase Fold and No Enzymatic Activity.
Structure, 17:139-, 2009

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.

PubMed: 19141290
DOI: 10.1016/J.STR.2008.11.005

Experimental method

X-RAY DIFFRACTION (1.97 Å)