6YCZ
Plasmodium falciparum Myosin A delta-Nter, Post-Rigor state
Summary for 6YCZ
Entry DOI | 10.2210/pdb6ycz/pdb |
Descriptor | Myosin-A, Myosin A tail domain interacting protein, Uncharacterized protein, ... (8 entities in total) |
Functional Keywords | myosin a, myosin, plasmodium, myosin xiv, myosin 14, motor protein |
Biological source | Plasmodium falciparum (isolate 3D7) More |
Total number of polymer chains | 3 |
Total formula weight | 132461.69 |
Authors | Moussaoui, D.,Robblee, J.P.,Auguin, D.,Krementsova, E.B.,Robert-Paganin, J.,Trybus, K.M.,Houdusse, A. (deposition date: 2020-03-19, release date: 2020-11-11, Last modification date: 2024-01-24) |
Primary citation | Moussaoui, D.,Robblee, J.P.,Auguin, D.,Krementsova, E.B.,Haase, S.,Blake, T.C.A.,Baum, J.,Robert-Paganin, J.,Trybus, K.M.,Houdusse, A. Full-length Plasmodium falciparum myosin A and essential light chain PfELC structures provide new anti-malarial targets. Elife, 9:-, 2020 Cited by PubMed Abstract: Parasites from the genus Plasmodium are the causative agents of malaria. The mobility, infectivity, and ultimately pathogenesis of rely on a macromolecular complex, called the glideosome. At the core of the glideosome is an essential and divergent Myosin A motor (PfMyoA), a first order drug target against malaria. Here, we present the full-length structure of PfMyoA in two states of its motor cycle. We report novel interactions that are essential for motor priming and the mode of recognition of its two light chains (PfELC and MTIP) by two degenerate IQ motifs. Kinetic and motility assays using PfMyoA variants, along with molecular dynamics, demonstrate how specific priming and atypical sequence adaptations tune the motor's mechano-chemical properties. Supported by evidence for an essential role of the PfELC in malaria pathogenesis, these structures provide a blueprint for the design of future anti-malarials targeting both the glideosome motor and its regulatory elements. PubMed: 33046215DOI: 10.7554/eLife.60581 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.27 Å) |
Structure validation
Download full validation report