+Open data
-Basic information
Entry | Database: PDB / ID: 6tu7 | |||||||||
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Title | Structure of PfMyoA decorated Plasmodium Act1 filament | |||||||||
Components |
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Keywords | MOTOR PROTEIN / malaria / Plasmodium falciparum / myosin / unconventional / filament | |||||||||
Function / homology | Function and homology information plastid inheritance / schizogony / pellicle / glideosome / inner membrane pellicle complex / symbiont-mediated actin polymerization-dependent cell-to-cell migration in host / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Neutrophil degranulation / entry into host cell by a symbiont-containing vacuole / myosin complex ...plastid inheritance / schizogony / pellicle / glideosome / inner membrane pellicle complex / symbiont-mediated actin polymerization-dependent cell-to-cell migration in host / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Neutrophil degranulation / entry into host cell by a symbiont-containing vacuole / myosin complex / microfilament motor activity / cytoskeletal motor activity / cytoskeleton organization / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / actin filament binding / actin cytoskeleton / actin binding / ATP hydrolysis activity / ATP binding / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Plasmodium falciparum 3D7 (eukaryote) | |||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Vahokoski, J. / Calder, L.J. / Lopez, A.J. / Rosenthal, P.B. / Kursula, I. | |||||||||
Funding support | Norway, United Kingdom, 2items
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Citation | Journal: PLoS Pathog / Year: 2022 Title: High-resolution structures of malaria parasite actomyosin and actin filaments. Authors: Juha Vahokoski / Lesley J Calder / Andrea J Lopez / Justin E Molloy / Inari Kursula / Peter B Rosenthal / 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 ...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. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6tu7.cif.gz | 538.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6tu7.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6tu7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6tu7_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 6tu7_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 6tu7_validation.xml.gz | 91.6 KB | Display | |
Data in CIF | 6tu7_validation.cif.gz | 133.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tu/6tu7 ftp://data.pdbj.org/pub/pdb/validation_reports/tu/6tu7 | HTTPS FTP |
-Related structure data
Related structure data | 10590MC 6tu4C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 92675.477 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum 3D7 (eukaryote) / Gene: PF13_0233 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q8IDR3 #2: Protein | Mass: 42047.676 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum 3D7 (eukaryote) / Gene: PFL2215w / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q8I4X0 #3: Chemical | ChemComp-ADP / #4: Chemical | ChemComp-MG / #5: Chemical | ChemComp-9UE / Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
-Sample preparation
Component | Name: PfMyoA decorated PfAct1 filament / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Plasmodium falciparum 3D7 (eukaryote) |
Source (recombinant) | Organism: Spodoptera frugiperda (fall armyworm) / Cell: Sf21 |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 49.2 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
Software |
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EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -166.498 ° / Axial rise/subunit: 28.3417 Å / Axial symmetry: C1 | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 239021 / Symmetry type: HELICAL | ||||||||||||||||||||||||
Atomic model building | Space: REAL | ||||||||||||||||||||||||
Atomic model building |
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Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 63.35 Å2 | ||||||||||||||||||||||||
Refine LS restraints |
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