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- EMDB-8951: PTEX Core Complex in the Engaged (Extended) State -

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Basic information

Entry
Database: EMDB / ID: EMD-8951
TitlePTEX Core Complex in the Engaged (Extended) State
Map dataPTEX Core Complex in the Engaged (Extended) State
Sample
  • Complex: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
    • Protein or peptide: Heat shock protein 101Heat shock response
    • Protein or peptide: Exported protein 2
    • Protein or peptide: Translocon component PTEX150
    • Protein or peptide: Endogenous cargo polypeptide
    • Protein or peptide: Unknown (Claw)
  • Ligand: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Function / homology
Function and homology information


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
ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp amino terminal domain, pathogenicity island component / Clp repeat (R) domain profile. / Clp, repeat (R) domain / Clp, N-terminal domain superfamily ...ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp amino terminal domain, pathogenicity island component / Clp repeat (R) domain profile. / Clp, repeat (R) domain / Clp, N-terminal domain superfamily / ClpA/B family / Clp ATPase, C-terminal / AAA domain (Cdc48 subfamily) / C-terminal, D2-small domain, of ClpB protein / C-terminal, D2-small domain, of ClpB protein / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Heat shock protein 101 / Exported protein 2 / Translocon component PTEX150
Similarity search - Component
Biological speciesPlasmodium falciparum 3D7 (eukaryote) / isolate 3D7 (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.16 Å
AuthorsHo C / Lai M / Zhou ZH
Funding support United States, 11 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R21 AI125983 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)T32 AI007323 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM071940 United States
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)R01 DE025567 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI094386 United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)S10RR23057 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)K99/R00 HL133453 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24GM116792 United States
National Institutes of Health/Office of the DirectorS10OD018111 United States
National Science Foundation (NSF, United States)DMR-1548924 United States
National Science Foundation (NSF, United States)DBI-1338135 United States
CitationJournal: Nature / Year: 2018
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
DepositionJul 8, 2018-
Header (metadata) releaseAug 22, 2018-
Map releaseAug 22, 2018-
UpdateNov 27, 2019-
Current statusNov 27, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.038
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.038
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6e10
  • Surface level: 0.038
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_8951.png

Downloads & links

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Map

FileDownload / File: emd_8951.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPTEX Core Complex in the Engaged (Extended) State
Voxel sizeX=Y=Z: 1.04 Å
Density
Contour LevelBy AUTHOR: 0.0424 / Movie #1: 0.038
Minimum - Maximum-0.062355958 - 0.13751948
Average (Standard dev.)0.00031809916 (±0.0034089806)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 499.19998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.041.041.04
M x/y/z480480480
origin x/y/z0.0000.0000.000
length x/y/z499.200499.200499.200
α/β/γ90.00090.00090.000
start NX/NY/NZ-69-50-137
NX/NY/NZ136114193
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS480480480
D min/max/mean-0.0620.1380.000

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Supplemental data

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Additional map: PTEX Core Complex in the Engaged (Extended) State, additional map #1

Fileemd_8951_additional_1.map
AnnotationPTEX Core Complex in the Engaged (Extended) State, additional map #1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: PTEX Core Complex in the Engaged (Extended) State, additional map #2

Fileemd_8951_additional_2.map
AnnotationPTEX Core Complex in the Engaged (Extended) State, additional map #2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Plasmodium Translocon of Exported Proteins (PTEX) Core Complex

EntireName: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
Components
  • Complex: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
    • Protein or peptide: Heat shock protein 101Heat shock response
    • Protein or peptide: Exported protein 2
    • Protein or peptide: Translocon component PTEX150
    • Protein or peptide: Endogenous cargo polypeptide
    • Protein or peptide: Unknown (Claw)
  • Ligand: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER

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Supramolecule #1: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex

SupramoleculeName: Plasmodium Translocon of Exported Proteins (PTEX) Core Complex
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)

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Macromolecule #1: Heat shock protein 101

MacromoleculeName: Heat shock protein 101 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: isolate 3D7 (eukaryote)
Molecular weightTheoretical: 106.277125 KDa
SequenceString: 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

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Macromolecule #2: Exported protein 2

MacromoleculeName: Exported protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: isolate 3D7 (eukaryote)
Molecular weightTheoretical: 33.458707 KDa
SequenceString: 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

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Macromolecule #3: Translocon component PTEX150

MacromoleculeName: Translocon component PTEX150 / type: protein_or_peptide / ID: 3 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: isolate 3D7 (eukaryote)
Molecular weightTheoretical: 22.59317 KDa
SequenceString: 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)

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Macromolecule #4: Endogenous cargo polypeptide

MacromoleculeName: Endogenous cargo polypeptide / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: isolate 3D7 (eukaryote)
Molecular weightTheoretical: 1.294587 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #5: Unknown (Claw)

MacromoleculeName: Unknown (Claw) / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: isolate 3D7 (eukaryote)
Molecular weightTheoretical: 4.954098 KDa
SequenceString: (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)

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Macromolecule #6: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 6 / Number of copies: 12 / Formula: AGS
Molecular weightTheoretical: 523.247 Da
Chemical component information

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
GridMaterial: COPPER / Support film - Material: CARBON / Support film - topology: LACEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
DetailsPTEX core complex purified from P. falciparum parasites cultured in human erythrocytes

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: 4.0 µm / Calibrated defocus min: 1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 130000
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm 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
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1508462
CTF correctionSoftware - Name: CTFFIND (ver. CTFFIND4.1)
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC
Final 3D classificationSoftware - Name: RELION (ver. 2.0)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.16 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 72866

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-6e10:
PTEX Core Complex in the Engaged (Extended) State

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