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PMID:19000816

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Citation

Kursula, I, Kursula, P, Ganter, M, Panjikar, S, Matuschewski, K and Schüler, H (2008) Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum. Structure 16:1638-48

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.

Links

PubMed Online version:10.1016/j.str.2008.09.008

Keywords

Amino Acid Sequence; Animals; Apicomplexa/genetics; Binding Sites; Conserved Sequence; Genetic Variation; Malaria, Falciparum/genetics; Models, Molecular; Molecular Sequence Data; Plasmodium/genetics; Plasmodium falciparum/genetics; Plasmodium falciparum/pathogenicity; Profilins/chemistry; Profilins/genetics; Proline/metabolism; Protein Conformation; Protozoan Proteins/chemistry; Protozoan Proteins/genetics; Sequence Alignment; Sequence Homology, Amino Acid

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:PROF1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P60709

F

Seeded From UniProt

complete

HUMAN:ACTB

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P07737

F

Seeded From UniProt

complete

HUMAN:ACTB

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P86294

F

Seeded From UniProt

complete

PLAFX:PROF

enables

GO:0005543: phospholipid binding

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

PLAFX:PROF

involved_in

GO:0030036: actin cytoskeleton organization

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

PLAFX:PROF

located_in

GO:0015629: actin cytoskeleton

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

PLAFX:PROF

enables

GO:0003779: actin binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P60709

F

Seeded From UniProt

complete

PLAFX:PROF

enables

GO:0003785: actin monomer binding

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

PLAFX:PROF

involved_in

GO:0060327: cytoplasmic actin-based contraction involved in cell motility

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:ACTB

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P60709

F

Seeded From UniProt

complete

See also

References

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