ArticlePLoS biology2019
Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover.Nature communications · 2024Article
- Article
- Sulfonylpiperazine compounds prevent Plasmodium falciparum invasion of red blood cells through interference with actin-1/profilin dynamics.PLoS biology · 2023Article
- Structure and function of Plasmodium actin II in the parasite mosquito stages.PLoS pathogens · 2023Article
- Divergent Plasmodium actin residues are essential for filament localization, mosquito salivary gland invasion and malaria transmission.PLoS pathogens · 2022Article
- Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.Nature communications · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- Structure and function of an atypical homodimeric actin capping protein from the malaria parasite.Cellular and molecular life sciences : CMLS · 2022Article
- The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.Nature communications · 2021Article
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium actins form very short filaments and have a noncanonical link between ATP hydrolysis and polymerization. Long filaments are detrimental to the parasites, but the structural factors constraining Plasmodium microfilament lengths have remained unknown. Using high-resolution crystallography, we show that magnesium binding causes a slight flattening of the Plasmodium actin I monomer, and subsequent phosphate release results in a more twisted conformation. Thus, the Mg-bound monomer is closer in conformation to filamentous (F) actin than the Ca form, and this likely facilitates polymerization. A coordinated potassium ion resides in the active site during hydrolysis and leaves together with the phosphate, a process governed by the position of the Arg178/Asp180-containing A loop. Asp180 interacts with either Lys270 or His74, depending on the protonation state of the histidine, while Arg178 links the inner and outer domains (ID and OD) of the actin protomer. Hence, the A loop acts as a switch between stable and unstable filament conformations, the latter leading to fragmentation. Our data provide a comprehensive model for polymerization, ATP hydrolysis and phosphate release, and fragmentation of parasite microfilaments. Similar mechanisms may well exist in canonical actins, although fragmentation is much less favorable due to several subtle sequence differences as well as the methylation of His73, which is absent on the corresponding His74 in Plasmodium actin I.
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