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- EMDB-11818: Cryo-EM structure of the divergent actomyosin complex from Plasmo... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-11818 | ||||||||||||
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Title | Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state | ||||||||||||
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Function / homology | ![]() 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 | ![]() ![]() | ||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.77 Å | ||||||||||||
![]() | Robert-Paganin J / Xu X-P / Swift MF / Auguin D / Robblee JP / Lu H / Fagnant PM / Krementsova EB / Trybus KM / Houdusse A ...Robert-Paganin J / Xu X-P / Swift MF / Auguin D / Robblee JP / Lu H / Fagnant PM / Krementsova EB / Trybus KM / Houdusse A / Volkmann N / Hanein D | ||||||||||||
Funding support | 3 items
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![]() | ![]() Title: The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity. Authors: Julien Robert-Paganin / Xiao-Ping Xu / Mark F Swift / Daniel Auguin / James P Robblee / Hailong Lu / Patricia M Fagnant / Elena B Krementsova / Kathleen M Trybus / Anne Houdusse / Niels ...Authors: Julien Robert-Paganin / Xiao-Ping Xu / Mark F Swift / Daniel Auguin / James P Robblee / Hailong Lu / Patricia M Fagnant / Elena B Krementsova / Kathleen M Trybus / Anne Houdusse / Niels Volkmann / Dorit Hanein / ![]() ![]() Abstract: Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these ...Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these interactions remained elusive until now. Here, we report an atomic structure of the divergent Plasmodium falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (Rigor state). The structure provides insights into the detailed interactions that are required for the parasite to produce the force and motion required for infectivity. Remarkably, the footprint of the myosin motor on filamentous actin is conserved with respect to higher eukaryotes, despite important variability in the Plasmodium falciparum myosin and actin elements that make up the interface. Comparison with other actomyosin complexes reveals a conserved core interface common to all actomyosin complexes, with an ancillary interface involved in defining the spatial positioning of the motor on actin filaments. | ||||||||||||
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 | ![]() | 14.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.7 KB 13.7 KB | Display Display | ![]() |
Images | ![]() | 275.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7alnMC 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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Voxel size | X=Y=Z: 1.035 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : actomyosin complex from Plasmodium falciparum
Entire | Name: actomyosin complex from Plasmodium falciparum |
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Components |
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-Supramolecule #1: actomyosin complex from Plasmodium falciparum
Supramolecule | Name: actomyosin complex from Plasmodium falciparum / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | 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: 41.919547 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGEEDVQALV VDNGSGNVKA GVAGDDAPRS VFPSIVGRPK NPGIMVGMEE KDAFVGDEAQ TKRGILTLKY PIEHGIVTNW DDMEKIWHH TFYNELRAAP EEHPVLLTEA PLNPKGNRER MTQIMFESFN VPAMYVAIQA VLSLYSSGRT TGIVLDSGDG V SHTVPIYE ...String: MGEEDVQALV VDNGSGNVKA GVAGDDAPRS VFPSIVGRPK NPGIMVGMEE KDAFVGDEAQ TKRGILTLKY PIEHGIVTNW DDMEKIWHH TFYNELRAAP EEHPVLLTEA PLNPKGNRER MTQIMFESFN VPAMYVAIQA VLSLYSSGRT TGIVLDSGDG V SHTVPIYE GYALPHAIMR LDLAGRDLTE YLMKILHERG YGFSTSAEKE IVRDIKEKLC YIALNFDEEM KTSEQSSDIE KS YELPDGN IITVGNERFR CPEALFQPSF LGKEAAGIHT TTFNSIKKCD VDIRKDLYGN IVLSGGTTMY EGIGERLTRD ITT LAPSTM KIKVVAPPER KYSVWIGGSI LSSLSTFQQM WITKEEYDES GPSIVHRKCF |
-Macromolecule #2: Myosin-A
Macromolecule | Name: Myosin-A / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 92.488289 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAVTNEEIKT ASKIVRRV(SEP)N VEAFDKSGSV FKGYQIWTDI SPTIENDPNI MFVKCVVQQG SKKEKLTVVQ IDPPGT GTP YDIDPTHAWN CNSQVDPMSF GDIGLLNHTN IPCVLDFLKH RYLKNQIYTT AVPLIVAINP YKDLGNTTNE WIRRYRD TA DHTKLPPHVF ...String: MAVTNEEIKT ASKIVRRV(SEP)N VEAFDKSGSV FKGYQIWTDI SPTIENDPNI MFVKCVVQQG SKKEKLTVVQ IDPPGT GTP YDIDPTHAWN CNSQVDPMSF GDIGLLNHTN IPCVLDFLKH RYLKNQIYTT AVPLIVAINP YKDLGNTTNE WIRRYRD TA DHTKLPPHVF TCAREALSNL HGVNKSQTII VSGESGAGKT EATKQIMRYF ASSKSGNMDL RIQTAIMAAN PVLEAFGN A KTIRNNNSSR FGRFMQLVIS HEGGIRYGSV VAFLLEKSRI ITQDDNERSY HIFYQFLKGA NSTMKSKFGL KGVTEYKLL NPNSTEVSGV DDVKDFEEVI ESLKNMELSE SDIEVIFSIV AGILTLGNVR LIEKQEAGLS DAAAIMDEDM GVFNKACELM YLDPELIKR EILIKVTVAG GDKIEGRWNK NDAEVLKSSL CKAMYEKLFL WIIRHLNSRI EPEGGFKTFM GMLDIFGFEV F KNNSLEQL FINITNEMLQ KNFVDIVFER ESKLYKDEGI STAELKYTSN KEVINVLCEK GKSVLSYLED QCLAPGGTDE KF VSSCATN LKENNKFTPA KVASNKNFII QHTIGPIQYC AESFLLKNKD VLRGDLVEVI KDSPNPIVQQ LFEGQVIEKG KIA KGSLIG SQFLNQLTSL MNLINSTEPH FIRCIKPNEN KKPLEWCEPK ILIQLHALSI LEALVLRQLG YSYRRTFEEF LYQY KFVDI AAAEDSSVEN QNKCVNILKL SGLSESMYKI GKSMVFLKQE GAKILTKIQR EKLVEWENCV SVIEAAILKH KYKQK VNKN IPSLLRVQAH IRKKMVAQ |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 5 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 5 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: Jasplakinolide
Macromolecule | Name: Jasplakinolide / type: ligand / ID: 5 / Number of copies: 3 / Formula: 9UE |
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Molecular weight | Theoretical: 709.67 Da |
Chemical component information | ![]() ChemComp-9UE: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.4 |
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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 II (4k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / 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: 27.3 Å Applied symmetry - Helical parameters - Δ&Phi: -168.1 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 464646 |
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Startup model | Type of model: OTHER / Details: in-house rabbit actin map filtered to 40A |
Final angle assignment | Type: NOT APPLICABLE |