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- EMDB-10590: Structure of PfMyoA decorated Plasmodium Act1 filament -

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Basic information

Entry
Database: EMDB / ID: EMD-10590
TitleStructure of PfMyoA decorated Plasmodium Act1 filament
Map dataGlobal B-factor sharpening
Sample
  • Complex: PfMyoA decorated PfAct1 filament
    • Protein or peptide: Myosin-A
    • Protein or peptide: Actin-1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: Jasplakinolide
Function / homology
Function and homology information


plastid inheritance / schizogony / pellicle / inner membrane pellicle complex / glideosome / 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 / inner membrane pellicle complex / glideosome / 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
Class XIV myosin, motor domain / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / Kinesin motor domain superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site ...Class XIV myosin, motor domain / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / Kinesin motor domain superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesPlasmodium falciparum 3D7 (eukaryote)
Methodhelical reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsVahokoski J / Calder LJ / Lopez AJ / Rosenthal PB / Kursula I
Funding support Norway, United Kingdom, 2 items
OrganizationGrant numberCountry
Norwegian Research Council Norway
The Francis Crick Institute United Kingdom
CitationJournal: 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
DepositionJan 3, 2020-
Header (metadata) releaseJan 13, 2021-
Map releaseJan 13, 2021-
UpdateAug 17, 2022-
Current statusAug 17, 2022Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.028
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.028
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6tu7
  • Surface level: 0.028
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6tu7
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10590.png

Downloads & links

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Map

FileDownload / File: emd_10590.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationGlobal B-factor sharpening
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 512 pix.
= 558.08 Å		1.09 Å/pix.
x 512 pix.
= 558.08 Å		1.09 Å/pix.
x 512 pix.
= 558.08 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.028 / Movie #1: 0.028
Minimum - Maximum-0.11581818 - 0.2643423
Average (Standard dev.)0.00047903805 (±0.00556916)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 558.08 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z558.080558.080558.080
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS512512512
D min/max/mean-0.1160.2640.000

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Supplemental data

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Mask #1

Fileemd_10590_msk_1.map
Projections & Slices
AxesZYX

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Additional map: #1

Fileemd_10590_additional_1.map
Projections & Slices
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Half map: #2

Fileemd_10590_half_map_1.map
Projections & Slices
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Histogram

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Half map: #1

Fileemd_10590_half_map_2.map
Projections & Slices
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Sample components

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Entire : PfMyoA decorated PfAct1 filament

EntireName: PfMyoA decorated PfAct1 filament
Components
  • Complex: PfMyoA decorated PfAct1 filament
    • Protein or peptide: Myosin-A
    • Protein or peptide: Actin-1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: Jasplakinolide

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Supramolecule #1: PfMyoA decorated PfAct1 filament

SupramoleculeName: PfMyoA decorated PfAct1 filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm) / Recombinant cell: Sf21

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Macromolecule #1: Myosin-A

MacromoleculeName: Myosin-A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)
Molecular weightTheoretical: 92.675477 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: GQFAVTNEEI KTASKIVRRV (SEP)NVEAFDKSG SVFKGYQIWT DISPTIENDP NIMFVKCVVQ QGSKKEKLTV VQIDPP GTG TPYDIDPTHA WNCNSQVDPM SFGDIGLLNH TNIPCVLDFL KHRYLKNQIY TTAVPLIVAI NPYKDLGNTT NEWIRRY RD TADHTKLPPH ...String:
GQFAVTNEEI KTASKIVRRV (SEP)NVEAFDKSG SVFKGYQIWT DISPTIENDP NIMFVKCVVQ QGSKKEKLTV VQIDPP GTG TPYDIDPTHA WNCNSQVDPM SFGDIGLLNH TNIPCVLDFL KHRYLKNQIY TTAVPLIVAI NPYKDLGNTT NEWIRRY RD TADHTKLPPH VFTCAREALS NLHGVNKSQT IIVSGESGAG KTEATKQIMR YFASSKSGNM DLRIQTAIMA ANPVLEAF G NAKTIRNNNS SRFGRFMQLV ISHEGGIRYG SVVAFLLEKS RIITQDDNER SYHIFYQFLK GANSTMKSKF GLKGVTEYK LLNPNSTEVS GVDDVKDFEE VIESLKNMEL SESDIEVIFS IVAGILTLGN VRLIEKQEAG LSDAAAIMDE DMGVFNKACE LMYLDPELI KREILIKVTV AGGTKIEGRW NKNDAEVLKS SLCKAMYEKL FLWIIRHLNS RIEPEGGFKT FMGMLDIFGF E VFKNNSLE QLFINITNEM LQKNFVDIVF ERESKLYKDE GISTAELKYT SNKEVINVLC EKGKSVLSYL EDQCLAPGGT DE KFVSSCA TNLKENNKFT PAKVASNKNF IIQHTIGPIQ YCAESFLLKN KDVLRGDLVE VIKDSPNPIV QQLFEGQVIE KGK IAKGSL IGSQFLNQLT SLMNLINSTE PHFIRCIKPN ENKKPLEWCE PKILIQLHAL SILEALVLRQ LGYSYRRTFE EFLY QYKFV DIAAAEDSSV ENQNKCVNIL KLSGLSESMY KIGKSMVFLK QEGAKILTKI QREKLVEWEN CVSVIEAAIL KHKYK QKVN KNIPSLLRVQ AHIRKKMVAQ

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Macromolecule #2: Actin-1

MacromoleculeName: Actin-1 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)
Molecular weightTheoretical: 42.047676 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: 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

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Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #5: Jasplakinolide

MacromoleculeName: Jasplakinolide / type: ligand / ID: 5 / Number of copies: 4 / Formula: 9UE
Molecular weightTheoretical: 709.67 Da
Chemical component information

ChemComp-9UE:
Jasplakinolide

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 49.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 28.3417 Å
Applied symmetry - Helical parameters - Δ&Phi: -166.498 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0 beta) / Number images used: 239021
Startup modelType of model: OTHER / Details: a cylinder
Final angle assignmentType: NOT APPLICABLE

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Atomic model buiding 1

Initial model
PDB IDChain

5ogw

chain_id: A

6i7d

chain_id: D
RefinementSpace: REAL
Output model

PDB-6tu7:
Structure of PfMyoA decorated Plasmodium Act1 filament

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