2JKG

Plasmodium falciparum profilin

Summary for 2JKG

• Entry DOI: 10.2210/pdb2jkg/pdb
• Related: 2JKF
• Descriptor: PROFILIN, OCTAPROLINE PEPTIDE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: proline-rich ligand, protein-binding, malaria, cytoskeleton, protein binding
• Biological source: PLASMODIUM FALCIPARUM; More
• Total number of polymer chains: 2
• Total formula weight: 20921.25

Authors

Kursula, I.,Kursula, P.,Ganter, M.,Panjikar, S.,Matuschewski, K.,Schueler, H. (deposition date: 2008-08-28, release date: 2008-09-23, Last modification date: 2024-05-08)

Primary citation

Kursula, I.,Kursula, P.,Ganter, M.,Panjikar, S.,Matuschewski, K.,Schuler, H.
Structural Basis for Parasite-Specific Functions of the Divergent Profilin of Plasmodium Falciparum.
Structure, 16:1638-, 2008

PubMed Abstract: Profilins are key regulators of actin dynamics. They sequester actin monomers, forming a pool for rapid polymer formation stimulated by proteins such as formins. Apicomplexan parasites utilize a highly specialized microfilament system for motility and host cell invasion. Their genomes encode only a small number of divergent actin regulators. We present the first crystal structure of an apicomplexan profilin, that of the malaria parasite Plasmodium falciparum, alone and in complex with a polyproline ligand peptide. The most striking feature of Plasmodium profilin is a unique minidomain consisting of a large beta-hairpin extension common to all apicomplexan parasites, and an acidic loop specific for Plasmodium species. Reverse genetics in the rodent malaria model, Plasmodium berghei, suggests that profilin is essential for the invasive blood stages of the parasite. Together, our data establish the structural basis for understanding the functions of profilin in the malaria parasite.

PubMed: 19000816
DOI: 10.1016/J.STR.2008.09.008

Experimental method

X-RAY DIFFRACTION (1.89 Å)