7ALN

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

Summary for 7ALN

• Entry DOI: 10.2210/pdb7aln/pdb
• EMDB information: 11818
• Descriptor: Actin-1, Myosin-A, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: malaria, plasmodium falciparum, myosin a, invasion, actin 1, motor protein
• Biological source: Plasmodium falciparum (isolate 3D7); More
• Total number of polymer chains: 6
• Total formula weight: 306472.56

Authors

Robert-Paganin, J.,Xu, X.-P.,Swift, M.F.,Auguin, D.,Robblee, J.P.,Lu, H.,Fagnant, P.M.,Krementsova, E.B.,Trybus, K.M.,Houdusse, A.,Volkmann, N.,Hanein, D. (deposition date: 2020-10-06, release date: 2021-04-28, Last modification date: 2024-10-23)

Primary citation

Robert-Paganin, J.,Xu, X.P.,Swift, M.F.,Auguin, D.,Robblee, J.P.,Lu, H.,Fagnant, P.M.,Krementsova, E.B.,Trybus, K.M.,Houdusse, A.,Volkmann, N.,Hanein, D.
The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.
Nat Commun, 12:1892-1892, 2021

PubMed 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.

PubMed: 33767187
DOI: 10.1038/s41467-021-22093-4

Experimental method

ELECTRON MICROSCOPY (3.77 Å)