Nature Communications (Mar 2021)

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

  • 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,
  • Dorit Hanein

DOI
https://doi.org/10.1038/s41467-021-22093-4
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 11

Abstract

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Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.