7KIY

Plasmodium falciparum RhopH complex in soluble form

Summary for 7KIY

• Entry DOI: 10.2210/pdb7kiy/pdb
• EMDB information: 22890
• Descriptor: Cytoadherence linked asexual protein 3, High molecular weight rhoptry protein-2, High molecular weight rhoptry protein 3 (3 entities in total)
• Functional Keywords: plasmodium falciparum, malaria, rhoph complex, membrane protein
• Biological source: Plasmodium falciparum; More
• Total number of polymer chains: 3
• Total formula weight: 444928.33

Authors

Schureck, M.A.,Darling, J.E.,Merk, A.,Subramaniam, S.,Desai, S.A. (deposition date: 2020-10-25, release date: 2021-01-13, Last modification date: 2024-10-23)

Primary citation

Schureck, M.A.,Darling, J.E.,Merk, A.,Shao, J.,Daggupati, G.,Srinivasan, P.,Olinares, P.D.B.,Rout, M.P.,Chait, B.T.,Wollenberg, K.,Subramaniam, S.,Desai, S.A.
Malaria parasites use a soluble RhopH complex for erythrocyte invasion and an integral form for nutrient uptake.
Elife, 10:-, 2021

PubMed Abstract: Malaria parasites use the RhopH complex for erythrocyte invasion and channel-mediated nutrient uptake. As the member proteins are unique to Plasmodium spp., how they interact and traffic through subcellular sites to serve these essential functions is unknown. We show that RhopH is synthesized as a soluble complex of CLAG3, RhopH2, and RhopH3 with 1:1:1 stoichiometry. After transfer to a new host cell, the complex crosses a vacuolar membrane surrounding the intracellular parasite and becomes integral to the erythrocyte membrane through a PTEX translocon-dependent process. We present a 2.9 Å single-particle cryo-electron microscopy structure of the trafficking complex, revealing that CLAG3 interacts with the other subunits over large surface areas. This soluble complex is tightly assembled with extensive disulfide bonding and predicted transmembrane helices shielded. We propose a large protein complex stabilized for trafficking but poised for host membrane insertion through large-scale rearrangements, paralleling smaller two-state pore-forming proteins in other organisms.

PubMed: 33393463
DOI: 10.7554/eLife.65282

Experimental method

ELECTRON MICROSCOPY (2.92 Å)