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6I7D

Plasmodium falciparum Myosin A, post-rigor and rigor-like states

Summary for 6I7D
Entry DOI10.2210/pdb6i7d/pdb
DescriptorMyosin-A, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
Functional Keywordsmyosin a, plasmodium falciparum, tunable mechanism, motor protein
Biological sourcePlasmodium falciparum (isolate 3D7)
Total number of polymer chains4
Total formula weight346492.98
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 citationRobert-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: 31337750
DOI: 10.1038/s41467-019-11120-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.82 Å)
Structure validation

226707

건을2024-10-30부터공개중

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