6TU7
Structure of PfMyoA decorated Plasmodium Act1 filament
This is a non-PDB format compatible entry.
Summary for 6TU7
| Entry DOI | 10.2210/pdb6tu7/pdb |
| EMDB information | 10590 |
| Descriptor | Myosin-A, Actin-1, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | malaria, plasmodium falciparum, myosin, unconventional, filament, motor protein |
| Biological source | Plasmodium falciparum 3D7 More |
| Total number of polymer chains | 6 |
| Total formula weight | 358186.36 |
| Authors | Vahokoski, J.,Calder, L.J.,Lopez, A.J.,Rosenthal, P.B.,Kursula, I. (deposition date: 2020-01-03, release date: 2021-01-13, Last modification date: 2022-08-17) |
| Primary citation | 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 Cited by 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: 35377914DOI: 10.1371/journal.ppat.1010408 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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