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The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity

Author

Listed:
  • Julien Robert-Paganin

    (Structural Motility, Institut Curie, CNRS, UMR 144)

  • Xiao-Ping Xu

    (Scintillon Institute)

  • Mark F. Swift

    (Scintillon Institute)

  • Daniel Auguin

    (Structural Motility, Institut Curie, CNRS, UMR 144
    Université d’Orléans, INRAE, USC1328)

  • James P. Robblee

    (University of Vermont)

  • Hailong Lu

    (University of Vermont)

  • Patricia M. Fagnant

    (University of Vermont)

  • Elena B. Krementsova

    (University of Vermont)

  • Kathleen M. Trybus

    (University of Vermont)

  • Anne Houdusse

    (Structural Motility, Institut Curie, CNRS, UMR 144)

  • Niels Volkmann

    (Scintillon Institute
    Institut Pasteur)

  • Dorit Hanein

    (Scintillon Institute
    Institut Pasteur)

Abstract

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.

Suggested Citation

  • Julien Robert-Paganin & Xiao-Ping Xu & Mark F. Swift & Daniel Auguin & James P. Robblee & Hailong Lu & Patricia M. Fagnant & Elena B. Krementsova & Kathleen M. Trybus & Anne Houdusse & Niels Volkmann , 2021. "The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22093-4
    DOI: 10.1038/s41467-021-22093-4
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    Cited by:

    1. Charles Bayly-Jones & Christopher J. Lupton & Claudia Fritz & Hariprasad Venugopal & Daniel Ramsbeck & Michael Wermann & Christian Jäger & Alex Marco & Stephan Schilling & Dagmar Schlenzig & James C. , 2022. "Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Alessandro Grinzato & Daniel Auguin & Carlos Kikuti & Neha Nandwani & Dihia Moussaoui & Divya Pathak & Eaazhisai Kandiah & Kathleen M. Ruppel & James A. Spudich & Anne Houdusse & Julien Robert-Paganin, 2023. "Cryo-EM structure of the folded-back state of human β-cardiac myosin," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Dihia Moussaoui & James P. Robblee & Julien Robert-Paganin & Daniel Auguin & Fabio Fisher & Patricia M. Fagnant & Jill E. Macfarlane & Julia Schaletzky & Eddie Wehri & Christoph Mueller-Dieckmann & Ja, 2023. "Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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