The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
25 03 2021
25 03 2021
Historique:
received:
10
11
2020
accepted:
08
02
2021
entrez:
26
3
2021
pubmed:
27
3
2021
medline:
10
4
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33767187
doi: 10.1038/s41467-021-22093-4
pii: 10.1038/s41467-021-22093-4
pmc: PMC7994445
doi:
Substances chimiques
Actins
0
Protozoan Proteins
0
Actomyosin
9013-26-7
Myosins
EC 3.6.4.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1892Subventions
Organisme : NIAID NIH HHS
ID : R01 AI132378
Pays : United States
Organisme : NIH HHS
ID : S10 OD012372
Pays : United States
Organisme : NIH HHS
ID : S10 OD026926
Pays : United States
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