ArticleMolecular and biochemical parasitology2013
The compact conformation of the Plasmodium knowlesi myosin tail interacting protein MTIP in complex with the C-terminal helix of myosin A.
Article in Molecular and biochemical parasitology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Complementary crosstalk between palmitoylation and phosphorylation events in MTIP regulates its role duringFrontiers in cellular and infection microbiology · 2022Article
- A De novo Peptide from a High Throughput Peptide Library Blocks Myosin A -MTIP Complex Formation inInternational journal of molecular sciences · 2020Article
- Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex.Malaria journal · 2015Article
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.The Journal of biological chemistry · 2014Article
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Authors and funding
4 authors.
Funding
Abstract
The myosin motor of the malaria parasite's invasion machinery moves over actin fibers while it is making critical contacts with the myosin-tail interacting protein (MTIP). Previously, in a "compact" Plasmodium falciparum MTIP•MyoA complex, MTIP domains 2 (D2) and 3 (D3) make contacts with the MyoA helix, and the central helix is kinked, but in an "extended" Plasmodium knowlesi MTIP•MyoA complex only D3 interacts with the MyoA helix, and the central helix is fully extended. Here we report the crystal structure of the compact P. knowlesi MTIP•MyoA complex. It appears that, depending on the pH, P. knowlesi MTIP can adopt either the compact or the extended conformation to interact with MyoA. Only at pH values above ~7.0, can key hydrogen bonds can be formed by the imidazole group of MyoA His810 with an aspartate carboxylate from the hinge of MTIP and a lysine amino group of MyoA simultaneously.
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