ArticleCommunications biology2020
Structural role of essential light chains in the apicomplexan glideosome.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Potential Molecular Targets of the Broad-Range Antimicrobial Peptide Tyrothricin in the Apicomplexan ParasiteBiomedicines · 2026Article
- Functional dissection of prenyltransferases reveals roles in endocytosis and secretory vacuolar sorting in type 2-ME49 strain ofVirulence · 2024Article
- A database of calculated solution parameters for the AlphaFold predicted protein structures.Scientific reports · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- The synchrotron radiation source PETRA III and its future ultra-low-emittance upgrade PETRA IV.European physical journal plus · 2022Article
- Article
- Dynamically expressed genes provide candidate viability biomarkers in a model coccidian.PloS one · 2021Article
- Full-lengtheLife · 2020Article
- Structural role of essential light chains in the apicomplexan glideosome.Communications biology · 2020Article
- The Dynamic Roles of the Inner Membrane Complex in the Multiple Stages of the Malaria Parasite.Frontiers in cellular and infection microbiology · 2020Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gliding, a type of motility based on an actin-myosin motor, is specific to apicomplexan parasites. Myosin A binds two light chains which further interact with glideosome associated proteins and assemble into the glideosome. The role of individual glideosome proteins is unclear due to the lack of structures of larger glideosome assemblies. Here, we investigate the role of essential light chains (ELCs) in Toxoplasma gondii and Plasmodium falciparum and present their crystal structures as part of trimeric sub-complexes. We show that although ELCs bind a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. We suggest that ELCs enhance MyoA performance by inducing secondary structure in MyoA and thus stiffen its lever arm. Structural and biophysical analysis reveals that calcium binding has no influence on the structure of ELCs. Our work represents a further step towards understanding the mechanism of gliding in Apicomplexa.
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