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- PDB-7aln: Cryo-EM structure of the divergent actomyosin complex from Plasmo... -

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Basic information

Entry
Database: PDB / ID: 7aln
TitleCryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state
Components
  • Actin-1
  • Myosin-A
KeywordsMOTOR PROTEIN / Malaria / Plasmodium falciparum / Myosin A / invasion / Actin 1
Function / homology
Function and homology information


plastid inheritance / schizogony / pellicle / glideosome / inner membrane pellicle complex / Platelet degranulation / 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 ...plastid inheritance / schizogony / pellicle / glideosome / inner membrane pellicle complex / Platelet degranulation / 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 / vesicle transport along actin filament / 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 / vesicle / ATP hydrolysis activity / ATP binding / 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. / Actins signature 1. / Actin, conserved site / Actins signature 2. / Kinesin motor domain superfamily / 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. / Actins signature 1. / Actin, conserved site / Actins signature 2. / Kinesin motor domain superfamily / 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
Jasplakinolide / ADENOSINE-5'-DIPHOSPHATE / Actin-1 / Myosin-A
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.77 Å
AuthorsRobert-Paganin, J. / Xu, X.-P. / Swift, M.F. / Auguin, D. / Robblee, J.P. / Lu, H. / Fagnant, P.M. / Krementsova, E.B. / Trybus, K.M. / Houdusse, A. ...Robert-Paganin, J. / Xu, X.-P. / Swift, M.F. / Auguin, D. / Robblee, J.P. / Lu, H. / Fagnant, P.M. / Krementsova, E.B. / Trybus, K.M. / Houdusse, A. / Volkmann, N. / Hanein, D.
Funding support3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-AI132378
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)S10-OD012372
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)S10-OD026926
CitationJournal: Nat Commun / Year: 2021
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
DepositionOct 6, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 28, 2021Provider: repository / Type: Initial release

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Assembly

Deposited unit
A: Actin-1
B: Actin-1
C: Actin-1
D: Actin-1
E: Actin-1
F: Myosin-A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)306,47319
Polymers302,0866
Non-polymers4,38713
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area20450 Å2
ΔGint-161 kcal/mol
Surface area102610 Å2
MethodPISA

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Components

#1: Protein
Actin-1 / / Actin I


Mass: 41919.547 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (isolate 3D7) (eukaryote)
Strain: isolate 3D7 / Gene: PFL2215w / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q8I4X0
#2: Protein Myosin-A / PfM-A


Mass: 92488.289 Da / Num. of mol.: 1 / Mutation: T417D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (isolate 3D7) (eukaryote)
Strain: isolate 3D7 / Gene: PF13_0233 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q8IDR3
#3: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-9UE / Jasplakinolide


Mass: 709.670 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C36H45BrN4O6
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: actomyosin complex from Plasmodium falciparumMyofilament
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Plasmodium falciparum (isolate 3D7) (eukaryote)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 60 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -168.1 ° / Axial rise/subunit: 27.3 Å / Axial symmetry: C1
3D reconstructionResolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 464646 / Symmetry type: HELICAL

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