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- PDB-6zbg: Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, a... -

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Basic information

Entry
Database: PDB / ID: 6zbg
TitleMerozoite surface protein 1 (MSP-1) from Plasmodium falciparum, alternative conformation 4
Components
  • (Merozoite surface antigens) x 2
  • Merozoite surface protein 1
  • Merozoite surface protein-1
KeywordsMEMBRANE PROTEIN / Merozoite surface protein 1 / malaria / Plasmodium falciparum / MSP-1 / p190 / GPI-anchored membrane protein
Function / homology
Function and homology information


vacuolar membrane / side of membrane / extracellular region / plasma membrane
Similarity search - Function
Merozoite surface 1, C-terminal / Merozoite surface protein, EGF domain 1 / Merozoite surface protein 1 (MSP1) C-terminus / MSP1 EGF domain 1
Similarity search - Domain/homology
Merozoite surface protein 1 / Merozoite surface protein 1 / Merozoite surface protein 1 / Merozoite surface protein 1
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsDijkman, P.M. / Kudryashev, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
Alexander von Humboldt FoundationSofja Kovalevskaja Award to Mikhail Kudryashev Germany
Citation
Journal: Sci Adv / Year: 2021
Title: Structure of the merozoite surface protein 1 from .
Authors: Patricia M Dijkman / Tanja Marzluf / Yingyi Zhang / Shih-Ying Scott Chang / Dominic Helm / Michael Lanzer / Hermann Bujard / Mikhail Kudryashev /
Abstract: The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, ...The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in infection and immunity.
#1: Journal: Sci Adv / Year: 2021
Title: Structure of the merozoite surface protein 1 from Plasmodium falciparum
Authors: Dijkman, P.M. / Marzluf, T. / Zhang, Y. / Chang, S.Y.S. / Helm, D. / Lanzer, M. / Bujard, H. / Kudryashev, M.
History
DepositionJun 8, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 19, 2021Provider: repository / Type: Initial release
Revision 1.1Jun 23, 2021Group: Database references / Category: citation / citation_author
Revision 1.2Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_admin.last_update

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Assembly

Deposited unit
A: Merozoite surface antigens
B: Merozoite surface antigens
C: Merozoite surface protein-1
D: Merozoite surface protein 1


Theoretical massNumber of molelcules
Total (without water)191,6254
Polymers191,6254
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area18850 Å2
ΔGint-162 kcal/mol
Surface area63950 Å2
MethodPISA

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Components

#1: Protein Merozoite surface antigens / Merozoite surface protein 1 / PMMSA


Mass: 81773.539 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Subunit of the MSP-1 complex
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Gene: gp190/ MSA1/ MSP1/ PMMSA / Production host: Escherichia coli (E. coli) / References: UniProt: Q25922
#2: Protein Merozoite surface antigens / Merozoite surface protein 1 / PMMSA


Mass: 20217.637 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Subunit of the MSP-1 complex
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Gene: msp1 / Production host: Escherichia coli (E. coli) / References: UniProt: M1V901
#3: Protein Merozoite surface protein-1


Mass: 46390.676 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Subunit of the MSP-1 complex
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Gene: msp1 / Production host: Escherichia coli (E. coli) / References: UniProt: M1VNZ6
#4: Protein Merozoite surface protein 1


Mass: 43243.133 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Subunit of the MSP-1 complex
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Gene: msp1 / Production host: Escherichia coli (E. coli) / References: UniProt: C4PDY5
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Merozoite surface protein 1 (MSP-1) / Type: COMPLEX
Details: Heteromeric assembly of p83/30 fusion and p38/42 fusion of MSP-1 from Plasmodium falciparum (monomer), processed with SUB-1 protease into the MSP-1 complex composed of the subunits p83, p30, p38, and p42
Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: Heteromeric assembly of p83/30 fusion and p38/42 fusion of MSP-1 from Plasmodium falciparum (monomer), processed with SUB-1 protease into the MSP-1 complex composed of the subunits p83, p30, p38, and p42
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 FIELD / Nominal magnification: 130000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 64 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)
Image scansMovie frames/image: 40

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Processing

EM softwareName: cryoSPARC / Version: 2.5 / Category: 3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 116037 / Symmetry type: POINT

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