AI Article Synopsis
- The myosin motor in malaria parasites moves along actin fibers, interacting with myosin-tail interacting protein (MTIP) to facilitate invasion.
- In the compact structure of the Plasmodium knowlesi MTIP•MyoA complex, MTIP domains D2 and D3 engage with the MyoA helix, causing a kinked formation, while an extended structure shows only D3 interacting, leading to a fully extended central helix.
- The crystal structure analysis reveals that MTIP can shift between compact and extended conformations depending on pH levels, with key hydrogen bonds forming at pH values above 7.0.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3910325 | PMC |
| http://dx.doi.org/10.1016/j.molbiopara.2013.06.004 | DOI Listing |
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