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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-8951 | ||||||||||||||||||||||||||||||||||||
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Title | PTEX Core Complex in the Engaged (Extended) State | ||||||||||||||||||||||||||||||||||||
![]() | PTEX Core Complex in the Engaged (Extended) State | ||||||||||||||||||||||||||||||||||||
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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 | single particle reconstruction / cryo EM / Resolution: 4.16 Å | ||||||||||||||||||||||||||||||||||||
![]() | Ho C / Lai M / Zhou ZH | ||||||||||||||||||||||||||||||||||||
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 | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 27 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 25.4 KB 25.4 KB | Display Display | ![]() |
Images | ![]() | 164.2 KB | ||
Others | ![]() ![]() | 24.4 MB 22.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 340.2 KB | Display | ![]() |
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Full document | ![]() | 339.8 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 8.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6e10MC ![]() 8952C ![]() 6e11C C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | PTEX Core Complex in the Engaged (Extended) State | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: PTEX Core Complex in the Engaged (Extended) State, additional map #1
File | emd_8951_additional_1.map | ||||||||||||
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Annotation | PTEX Core Complex in the Engaged (Extended) State, additional map #1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: PTEX Core Complex in the Engaged (Extended) State, additional map #2
File | emd_8951_additional_2.map | ||||||||||||
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Annotation | PTEX Core Complex in the Engaged (Extended) State, additional map #2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
Entire | Name: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex |
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Components |
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-Supramolecule #1: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
Supramolecule | Name: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Heat shock protein 101
Macromolecule | Name: Heat shock protein 101 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 106.277125 KDa |
Sequence | String: MTRRYLKYYI FVTLLFFVQV INNVLCAPDN KQEQGKYLNR TINILNAGKN IAKSYGHNKL KPIHILSALA KSDYGSTLFK ENNVNAANL KEYIDIALEQ TRAGAPLDNK SKIVNSAEVK ETLALAEAAA NKYKSPKVDV EHLLSGLSND ELVNEIFNEV Y LTDEAIKA ...String: MTRRYLKYYI FVTLLFFVQV INNVLCAPDN KQEQGKYLNR TINILNAGKN IAKSYGHNKL KPIHILSALA KSDYGSTLFK ENNVNAANL KEYIDIALEQ TRAGAPLDNK SKIVNSAEVK ETLALAEAAA NKYKSPKVDV EHLLSGLSND ELVNEIFNEV Y LTDEAIKA ILKRKFEKTK KDKDGKTGTL YIEQFGSNMN EKVRNGKLQG IYGRDEEIRA IIESLLRYNK NSPVLVGNPG TG KTTIVEG LVYRIEKGDV PKELQGYTVI SLNFRKFTSG TSYRGEFETR MKNIIKELKN KKNKIILFVD EIHLLLGAGK AEG GTDAAN LLKPVLSKGE IKLIGATTIA EYRKFIESCS AFERRFEKIL VEPPSVDMTV KILRSLKSKY ENFYGINITD KALV AAAKI SDRFIKDRYL PDKAIDLLNK ACSFLQVQLS GKPRIIDVTE RDIERLSYEI STLEKDVDKV SKKKYNKLIK EFEEK KEQL KKYYEEYVIT GERLKRKKEI EKKLNDLKEL TQNYVYSNKE PPIELQNSLK EAQQKYLELY KETVAYVEAK THNAMN VDA VYQEHVSYIY LRDSGMPLGS LSFESSKGAL KLYNSLSKSI IGNEDIIKSL SDAVVKAATG MKDPEKPIGT FLFLGPT GV GKTELAKTLA IELFNSKDNL IRVNMSEFTE AHSVSKITGS PPGYVGFSDS GQLTEAVREK PHSVVLFDEL EKAHADVF K VLLQILGDGY INDNHRRNID FSNTIIIMTS NLGAELFKKK LFFDADNSGT PEYKRVMEDV RLSLIKKCKK VFKPEFVNR IDKIGVFEPL NKKNLHKIVA LRFKKLEKRL EEKNIQVSVS EKAIDYIIDQ SYDPELGARP TLIFIESVIM TKFAIMYLKK ELVDDMDVF VDYNSKAKNL VINLSKTPRD YKDDDDKDYK DDDDKDYKDD DDK |
-Macromolecule #2: Exported protein 2
Macromolecule | Name: Exported protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 33.458707 KDa |
Sequence | String: MKVSYIFSFF LLFFVYKNTN TVVCDNGYGD LAATSALTTV IKDPISLTIK DIYEHGVKNP FTKIIHKLKK FIRYRKVLRW SRMWWVLLV REIVGDNTIE KKTEKALREI WDQCTIAVYN NTLNAVESKP LLFLHGILNE CRNNFATKLR QDPSLIVAKI D QIIKSQIY ...String: MKVSYIFSFF LLFFVYKNTN TVVCDNGYGD LAATSALTTV IKDPISLTIK DIYEHGVKNP FTKIIHKLKK FIRYRKVLRW SRMWWVLLV REIVGDNTIE KKTEKALREI WDQCTIAVYN NTLNAVESKP LLFLHGILNE CRNNFATKLR QDPSLIVAKI D QIIKSQIY RFWVSEPYLK IGRSHTLYTH ITPDAVPQLP KECTLKHLSS YMEEKLKSME SKKNIESGKY EFDVDSSETD ST KDDGKPD DDDDDDDNFD DDDNFDDDTV EEEDASGDLF KNEKKDENKE |
-Macromolecule #3: Translocon component PTEX150
Macromolecule | Name: Translocon component PTEX150 / type: protein_or_peptide / ID: 3 / Number of copies: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 22.59317 KDa |
Sequence | String: SVKDIKKLIE EGILDYEDLT ENELRKLAKP DDNFYELSPY ASDEKDLSLN ETSGLTNEQL KNFLGQNGTY HMSYDSKSID YAKQKKSEK KEDQQEDDDG FYDAYKQIKN SYDGIPNNFN HEAPQLIGNN YVFTSIYDTK ENLIKFLKKN SEYDLYD (UNK)(UNK) (UNK) ...String: SVKDIKKLIE EGILDYEDLT ENELRKLAKP DDNFYELSPY ASDEKDLSLN ETSGLTNEQL KNFLGQNGTY HMSYDSKSID YAKQKKSEK KEDQQEDDDG FYDAYKQIKN SYDGIPNNFN HEAPQLIGNN YVFTSIYDTK ENLIKFLKKN SEYDLYD (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK) |
-Macromolecule #4: Endogenous cargo polypeptide
Macromolecule | Name: Endogenous cargo polypeptide / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 1.294587 KDa |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) |
-Macromolecule #5: Unknown (Claw)
Macromolecule | Name: Unknown (Claw) / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 4.954098 KDa |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) |
-Macromolecule #6: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 6 / Number of copies: 12 / Formula: AGS |
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Molecular weight | Theoretical: 523.247 Da |
Chemical component information | ![]() ChemComp-AGS: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Grid | Material: COPPER / Support film - Material: CARBON / Support film - topology: LACEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
Details | PTEX core complex purified from P. falciparum parasites cultured in human erythrocytes |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3710 pixel / Digitization - Dimensions - Height: 3838 pixel / Digitization - Frames/image: 2-50 / Average exposure time: 10.0 sec. / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 4.0 µm / Calibrated defocus min: 1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 130000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-6e10: |