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-Structure paper
タイトル | High-resolution structures of malaria parasite actomyosin and actin filaments. |
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ジャーナル・号・ページ | PLoS Pathog, Vol. 18, Issue 4, Page e1010408, Year 2022 |
掲載日 | 2022年4月4日 |
著者 | Juha Vahokoski / Lesley J Calder / Andrea J Lopez / Justin E Molloy / Inari Kursula / Peter B Rosenthal / |
PubMed 要旨 | 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 ...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. |
リンク | PLoS Pathog / PubMed:35377914 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.6 - 3.1 Å |
構造データ | EMDB-10587, PDB-6tu4: EMDB-10590, PDB-6tu7: |
化合物 | ChemComp-MG: ChemComp-9UE: ChemComp-ADP: ChemComp-HOH: |
由来 |
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キーワード | MOTOR PROTEIN (モータータンパク質) / malaria (マラリア) / Plasmodium falciparum / myosin (ミオシン) / unconventional (慣習) / filament |