7aln

Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state

spinqualitylabelsall models 7aln, resolution 3.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7aln is a 6 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.77Å Ligands: 9UE, ADP, MG, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACT1_PLAF7 Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility. Publication Abstract from PubMed Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these interactions remained elusive until now. Here, we report an atomic structure of the divergent Plasmodium falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (Rigor state). The structure provides insights into the detailed interactions that are required for the parasite to produce the force and motion required for infectivity. Remarkably, the footprint of the myosin motor on filamentous actin is conserved with respect to higher eukaryotes, despite important variability in the Plasmodium falciparum myosin and actin elements that make up the interface. Comparison with other actomyosin complexes reveals a conserved core interface common to all actomyosin complexes, with an ancillary interface involved in defining the spatial positioning of the motor on actin filaments. The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.,Robert-Paganin J, Xu XP, Swift MF, Auguin D, Robblee JP, Lu H, Fagnant PM, Krementsova EB, Trybus KM, Houdusse A, Volkmann N, Hanein D Nat Commun. 2021 Mar 25;12(1):1892. doi: 10.1038/s41467-021-22093-4. PMID:33767187 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

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