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TitleHigh-resolution structures of malaria parasite actomyosin and actin filaments.
Journal, issue, pagesPLoS Pathog, Vol. 18, Issue 4, Page e1010408, Year 2022
Publish dateApr 4, 2022
AuthorsJuha Vahokoski / Lesley J Calder / Andrea J Lopez / Justin E Molloy / Inari Kursula / Peter B Rosenthal /
PubMed AbstractMalaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon ...Malaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon an unconventional actomyosin motor for both gliding motility and host cell invasion. The motor system, often referred to as the glideosome complex, remains to be understood in molecular terms and is an attractive target for new drugs that might block the infection pathway. Here, we present the high-resolution structure of the actomyosin motor complex from Plasmodium falciparum. The complex includes the malaria parasite actin filament (PfAct1) complexed with the class XIV myosin motor (PfMyoA) and its two associated light-chains. The high-resolution core structure reveals the PfAct1:PfMyoA interface in atomic detail, while at lower-resolution, we visualize the PfMyoA light-chain binding region, including the essential light chain (PfELC) and the myosin tail interacting protein (PfMTIP). Finally, we report a bare PfAct1 filament structure at improved resolution.
External linksPLoS Pathog / PubMed:35377914 / PubMed Central
MethodsEM (helical sym.)
Resolution2.6 - 3.1 Å
Structure data

10587

6tu4

EMDB-10587, PDB-6tu4:
Structure of Plasmodium Actin1 filament
Method: EM (helical sym.) / Resolution: 2.6 Å

10590

6tu7

EMDB-10590, PDB-6tu7:
Structure of PfMyoA decorated Plasmodium Act1 filament
Method: EM (helical sym.) / Resolution: 3.1 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-9UE:
Jasplakinolide

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • plasmodium falciparum 3d7 (eukaryote)
KeywordsMOTOR PROTEIN / malaria / Plasmodium falciparum / myosin / unconventional / filament

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