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- PDB-6zbf: Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, a... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6zbf | ||||||
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Title | Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, alternative conformation 3 | ||||||
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![]() | MEMBRANE PROTEIN / Merozoite surface protein 1 / malaria / Plasmodium falciparum / MSP-1 / p190 / GPI-anchored membrane protein | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||
![]() | Dijkman, P.M. / Kudryashev, M. | ||||||
Funding support | ![]()
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![]() | ![]() 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: ![]() 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 |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 412.1 KB | Display | ![]() |
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PDB format | ![]() | 344.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 11153MC ![]() 6zbcC ![]() 6zbdC ![]() 6zbeC ![]() 6zbgC ![]() 6zbhC ![]() 6zbjC ![]() 6zblC M: map data used to model this data C: citing same article ( |
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Similar structure data | |
EM raw data | ![]() Data size: 34.0 TB Data #1: Unaligned movies of MSP-1 [micrographs - multiframe] Data #2: Unaligned movies of hdMSP-1 (dataset 1) [micrographs - multiframe] Data #3: Unaligned movies of hdMSP-1 (dataset 2) [micrographs - multiframe] Data #4: Unaligned movies of hdMSP-1 (dataset 3) [micrographs - multiframe] Data #5: Unaligned movies of hdMSP-1 (dataset 4) [micrographs - multiframe] Data #6: Final particle stack for hdMSP-1 conformation 1 [picked particles - single frame - processed] Data #7: Final particle stack for hdMSP-1 conformation 2 [picked particles - single frame - processed] Data #8: Final particle stack for MSP-1 main conformation [picked particles - single frame - processed] Data #9: Final particle stack for MSP-1 alternative conformation 1 [picked particles - single frame - processed] Data #10: Final particle stack for MSP-1 alternative conformation 2 [picked particles - single frame - processed] Data #11: Final particle stack for MSP-1 alternative conformation 3 [picked particles - single frame - processed] Data #12: Final particle stack for MSP-1 alternative conformation 4 [picked particles - single frame - processed] Data #13: Final particle stack for MSP-1 alternative conformation 5 [picked particles - single frame - processed]) |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | 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.) ![]() ![]() Gene: gp190/ MSA1/ MSP1/ PMMSA / Production host: ![]() ![]() |
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#2: Protein | 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.) ![]() ![]() Gene: msp1 / Production host: ![]() ![]() |
#3: Protein | 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.) ![]() ![]() Gene: msp1 / Production host: ![]() ![]() |
#4: Protein | 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.) ![]() ![]() Gene: msp1 / Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: 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 |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding 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 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 64 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
Image scans | Movie frames/image: 40 |
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Processing
EM software | Name: cryoSPARC / Version: 2.5 / Category: 3D reconstruction |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 124774 / Symmetry type: POINT |