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Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA from Toxoplasma gondii.


ABSTRACT: Parasites of the phylum Apicomplexa are responsible for significant morbidity and mortality on a global scale. Central to the virulence of these pathogens are the phylum-specific, unconventional class XIV myosins that power the essential processes of parasite motility and host cell invasion. Notably, class XIV myosins differ from human myosins in key functional regions, yet they are capable of fast movement along actin filaments with kinetics rivaling previously studied myosins. Toward establishing a detailed molecular mechanism of class XIV motility, we determined the 2.6-Å resolution crystal structure of the Toxoplasma gondii MyoA (TgMyoA) motor domain. Structural analysis reveals intriguing strategies for force transduction and chemomechanical coupling that rely on a divergent SH

SUBMITTER: Powell CJ 

PROVIDER: S-EPMC6233092 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature