6TU4

Structure of Plasmodium Actin1 filament

6TU4 の概要

• エントリーDOI: 10.2210/pdb6tu4/pdb
• EMDBエントリー: 10587
• 分子名称: Actin-1, MAGNESIUM ION, Jasplakinolide, ... (5 entities in total)
• 機能のキーワード: malaria, plasmodium falciparum, myosin, unconventional, filament, motor protein
• 由来する生物種: Plasmodium falciparum 3D7
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 216044.26

構造登録者

Vahokoski, J.,Calder, L.J.,Lopez, A.J.,Rosenthal, P.B.,Kursula, I. (登録日: 2020-01-02, 公開日: 2021-01-13, 最終更新日: 2024-07-10)

主引用文献

Vahokoski, J.,Calder, L.J.,Lopez, A.J.,Molloy, J.E.,Kursula, I.,Rosenthal, P.B.
High-resolution structures of malaria parasite actomyosin and actin filaments.
Plos Pathog., 18:e1010408-e1010408, 2022

PubMed Abstract: 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.

PubMed: 35377914
DOI: 10.1371/journal.ppat.1010408

実験手法

ELECTRON MICROSCOPY (2.6 Å)