9YA0

Cryo-EM structure of pre-conoid ring 2 (PCR P2 ring)from Toxoplasma gondii

This is a non-PDB format compatible entry.

Summary for 9YA0

• Entry DOI: 10.2210/pdb9ya0/pdb
• EMDB information: 72716
• Descriptor: PCR5, TGME49_242320, PCR12, TGME49_292170, PCR10, TGME49_298010, ... (20 entities in total)
• Functional Keywords: tubulin, microtubule, microtubule inner protein, microtubule-associated protein, toxoplasma gondii, conoid, conoid fiber, pre-conoid ring, pcr, p2, structural protein
• Biological source: Toxoplasma gondii; More
• Total number of polymer chains: 117
• Total formula weight: 23832884.44

Authors

Zeng, J.,Zhang, R. (deposition date: 2025-09-15, release date: 2025-11-19, Last modification date: 2025-12-24)

Primary citation

Zeng, J.,Fu, Y.,Qian, P.,Huang, W.,Niu, Q.,Beatty, W.L.,Brown, A.,Sibley, L.D.,Zhang, R.
Atomic models of the Toxoplasma cell invasion machinery.
Nat.Struct.Mol.Biol., 2025

PubMed Abstract: Apicomplexan parasites, responsible for toxoplasmosis, cryptosporidiosis and malaria, invade host cells through a unique gliding motility mechanism powered by actomyosin motors and a dynamic organelle called the conoid. Here, using cryo-electron microscopy, we determined structures of four essential complexes of the Toxoplasma gondii conoid: the preconoidal P2 ring, tubulin-based conoid fibers, and the subpellicular and intraconoidal microtubules. Our analysis identified 40 distinct conoid proteins, several of which are essential for parasite lytic growth, as revealed through genetic disruption studies. Comparative analysis of the tubulin-containing complexes sheds light on their functional specialization by microtubule-associated proteins, while the structure of the preconoidal ring pinpoints the site of actin polymerization and initial translocation, enhancing our mechanistic understanding of gliding motility and, therefore, parasite invasion.

PubMed: 41366525
DOI: 10.1038/s41594-025-01728-w

Experimental method

ELECTRON MICROSCOPY (3.54 Å)