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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10587 | |||||||||
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Title | Structure of Plasmodium Actin1 filament | |||||||||
![]() | global B-factor sharpening | |||||||||
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![]() | malaria / Plasmodium falciparum / myosin / unconventional / filament / MOTOR PROTEIN | |||||||||
Function / homology | ![]() plastid inheritance / schizogony / 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 / cytoskeleton organization / actin filament / structural constituent of cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement ...plastid inheritance / schizogony / 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 / cytoskeleton organization / actin filament / structural constituent of cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / actin cytoskeleton / ATP hydrolysis activity / ATP binding / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
![]() | Vahokoski J / Calder LJ | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() 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 |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.8 KB 17.8 KB | Display Display | ![]() |
Images | ![]() | 174.4 KB | ||
Masks | ![]() | 134.6 MB | ![]() | |
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() ![]() | 105.4 MB 105.6 MB 105.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 665.8 KB | Display | ![]() |
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Full document | ![]() | 665.4 KB | Display | |
Data in XML | ![]() | 14.1 KB | Display | |
Data in CIF | ![]() | 16.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6tu4MC ![]() 6tu7C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | global B-factor sharpening | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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-Additional map: #1
File | emd_10587_additional_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
File | emd_10587_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_10587_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : PfAct1 filament
Entire | Name: PfAct1 filament |
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Components |
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-Supramolecule #1: PfAct1 filament
Supramolecule | Name: PfAct1 filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Actin-1
Macromolecule | Name: Actin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 42.047676 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GAMGEEDVQA LVVDNGSGNV KAGVAGDDAP RSVFPSIVGR PKNPGIMVGM EEKDAFVGDE AQTKRGILTL KYPIEHGIVT NWDDMEKIW HHTFYNELRA APEEHPVLLT EAPLNPKGNR ERMTQIMFES FNVPAMYVAI QAVLSLYSSG RTTGIVLDSG D GVSHTVPI ...String: GAMGEEDVQA LVVDNGSGNV KAGVAGDDAP RSVFPSIVGR PKNPGIMVGM EEKDAFVGDE AQTKRGILTL KYPIEHGIVT NWDDMEKIW HHTFYNELRA APEEHPVLLT EAPLNPKGNR ERMTQIMFES FNVPAMYVAI QAVLSLYSSG RTTGIVLDSG D GVSHTVPI YEGYALPHAI MRLDLAGRDL TEYLMKILHE RGYGFSTSAE KEIVRDIKEK LCYIALNFDE EMKTSEQSSD IE KSYELPD GNIITVGNER FRCPEALFQP SFLGKEAAGI HTTTFNSIKK CDVDIRKDLY GNIVLSGGTT MYEGIGERLT RDI TTLAPS TMKIKVVAPP ERKYSVWIGG SILSSLSTFQ QMWITKEEYD ESGPSIVHRK CF UniProtKB: Actin-1 |
-Macromolecule #2: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 2 / Number of copies: 5 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #3: Jasplakinolide
Macromolecule | Name: Jasplakinolide / type: ligand / ID: 3 / Number of copies: 5 / Formula: 9UE |
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Molecular weight | Theoretical: 709.67 Da |
Chemical component information | ![]() ChemComp-9UE: |
-Macromolecule #4: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 5 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #5: water
Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 140 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 51.52 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 28.3692 Å Applied symmetry - Helical parameters - Δ&Phi: -167.652 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.7) / Number images used: 305480 |
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Startup model | Type of model: OTHER / Details: a cylinder |
Final angle assignment | Type: NOT APPLICABLE |