6I7D
Plasmodium falciparum Myosin A, post-rigor and rigor-like states
Summary for 6I7D
Entry DOI | 10.2210/pdb6i7d/pdb |
Descriptor | Myosin-A, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total) |
Functional Keywords | myosin a, plasmodium falciparum, tunable mechanism, motor protein |
Biological source | Plasmodium falciparum (isolate 3D7) |
Total number of polymer chains | 4 |
Total formula weight | 346492.98 |
Authors | Robert-Paganin, J.,Auguin, D.,Moussaoui, D.,Jousset, G.,Baum, J.,Trybus, K.M.,Houdusse, A. (deposition date: 2018-11-16, release date: 2019-08-07, Last modification date: 2024-01-24) |
Primary citation | Robert-Paganin, J.,Robblee, J.P.,Auguin, D.,Blake, T.C.A.,Bookwalter, C.S.,Krementsova, E.B.,Moussaoui, D.,Previs, M.J.,Jousset, G.,Baum, J.,Trybus, K.M.,Houdusse, A. Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism. Nat Commun, 10:3286-3286, 2019 Cited by PubMed Abstract: Plasmodium parasites are obligate intracellular protozoa and causative agents of malaria, responsible for half a million deaths each year. The lifecycle progression of the parasite is reliant on cell motility, a process driven by myosin A, an unconventional single-headed class XIV molecular motor. Here we demonstrate that myosin A from Plasmodium falciparum (PfMyoA) is critical for red blood cell invasion. Further, using a combination of X-ray crystallography, kinetics, and in vitro motility assays, we elucidate the non-canonical interactions that drive this motor's function. We show that PfMyoA motor properties are tuned by heavy chain phosphorylation (Ser19), with unphosphorylated PfMyoA exhibiting enhanced ensemble force generation at the expense of speed. Regulated phosphorylation may therefore optimize PfMyoA for enhanced force generation during parasite invasion or for fast motility during dissemination. The three PfMyoA crystallographic structures presented here provide a blueprint for discovery of specific inhibitors designed to prevent parasite infection. PubMed: 31337750DOI: 10.1038/s41467-019-11120-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.82 Å) |
Structure validation
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