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Open data
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Basic information
Entry | Database: PDB / ID: 600000000000 | ||||||||||||||||||||||||||||||||||||
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Title | PTEX Core Complex in the Resetting (Compact) State | ||||||||||||||||||||||||||||||||||||
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![]() | PROTEIN TRANSPORT / Translocon / Membrane Protein / ATPase | ||||||||||||||||||||||||||||||||||||
Function / homology | ![]() PTEX complex / apical complex / symbiont-containing vacuole / translocation of peptides or proteins into host cell cytoplasm / symbiont-containing vacuole membrane / response to unfolded protein / cellular response to heat / response to heat / ATP hydrolysis activity / ATP binding / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.23 Å | ||||||||||||||||||||||||||||||||||||
![]() | Ho, C. / Lai, M. / Zhou, Z.H. | ||||||||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Malaria parasite translocon structure and mechanism of effector export. Authors: Chi-Min Ho / Josh R Beck / Mason Lai / Yanxiang Cui / Daniel E Goldberg / Pascal F Egea / Z Hong Zhou / ![]() Abstract: The putative Plasmodium translocon of exported proteins (PTEX) is essential for transport of malarial effector proteins across a parasite-encasing vacuolar membrane into host erythrocytes, but the ...The putative Plasmodium translocon of exported proteins (PTEX) is essential for transport of malarial effector proteins across a parasite-encasing vacuolar membrane into host erythrocytes, but the mechanism of this process remains unknown. Here we show that PTEX is a bona fide translocon by determining structures of the PTEX core complex at near-atomic resolution using cryo-electron microscopy. We isolated the endogenous PTEX core complex containing EXP2, PTEX150 and HSP101 from Plasmodium falciparum in the 'engaged' and 'resetting' states of endogenous cargo translocation using epitope tags inserted using the CRISPR-Cas9 system. In the structures, EXP2 and PTEX150 interdigitate to form a static, funnel-shaped pseudo-seven-fold-symmetric protein-conducting channel spanning the vacuolar membrane. The spiral-shaped AAA+ HSP101 hexamer is tethered above this funnel, and undergoes pronounced compaction that allows three of six tyrosine-bearing pore loops lining the HSP101 channel to dissociate from the cargo, resetting the translocon for the next threading cycle. Our work reveals the mechanism of P. falciparum effector export, and will inform structure-based design of drugs targeting this unique translocon. | ||||||||||||||||||||||||||||||||||||
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 | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 150.7 KB | Display | |
Data in CIF | ![]() | 242.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8952MC ![]() 8951C ![]() 6e10C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Protein , 4 types, 27 molecules ijknhlm123456CDEBAGFdcbagfe
#1: Protein | Mass: 5124.308 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 103031.914 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: isolate 3D7 / References: UniProt: Q8IIJ8 #3: Protein | Mass: 33458.707 Da / Num. of mol.: 7 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: isolate 3D7 / References: UniProt: Q8IKC8 #5: Protein | Mass: 112523.328 Da / Num. of mol.: 7 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: isolate 3D7 / References: UniProt: Q8ILA1 |
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-Protein/peptide / Non-polymers , 2 types, 13 molecules 0![](data/chem/img/AGS.gif)
![](data/chem/img/AGS.gif)
#4: Protein/peptide | Mass: 528.644 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#6: Chemical | ChemComp-AGS / |
-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: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex Type: COMPLEX / Entity ID: #1-#5 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: PTEX core complex purified from P. falciparum parasites cultured in human erythrocytes |
Specimen support | Details: unspecified |
Vitrification | Instrument: FEI VITROBOT MARK IV / 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: 4000 nm / Nominal defocus min: 2000 nm / Calibrated defocus min: 1500 nm / Calibrated defocus max: 4000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 10 sec. / Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
EM imaging optics | Energyfilter name: GIF Quantum LS / Energyfilter upper: 10 eV / Energyfilter lower: -10 eV |
Image scans | Width: 3710 / Height: 3838 / Movie frames/image: 50 / Used frames/image: 2-50 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 1508462 | ||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.23 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 78499 / Algorithm: BACK PROJECTION / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL |