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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM of T2SS PulG pilus | |||||||||
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Sample |
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Keywords | Endopilus / T2SS / PulG / PROTEIN FIBRIL | |||||||||
| Function / homology | : Function and homology information | |||||||||
| Biological species | Klebsiella oxytoca (bacteria) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Sonani RR / Lejeune M / Ivashchenko S / Bardiaux B / Vos M / Francetic O / Shevchik VE / Izadi-Pruneyre N / Egelman EH | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Structure / Year: 2026Title: Structural determinants of endopilus assembly, stability, and functional specificity in bacterial type II secretion. Authors: Maylis Lejeune / Stefaniia Ivashchenko / Régine Dazzoni / Benjamin Bardiaux / Ravi R Sonani / Matthijn Vos / Theis Jacobsen / Edward H Egelman / Michael Nilges / Olivera Francetic / ...Authors: Maylis Lejeune / Stefaniia Ivashchenko / Régine Dazzoni / Benjamin Bardiaux / Ravi R Sonani / Matthijn Vos / Theis Jacobsen / Edward H Egelman / Michael Nilges / Olivera Francetic / Vladimir E Shevchik / Nadia Izadi-Pruneyre / ![]() Abstract: Gram-negative bacteria employ the type II secretion system (T2SS) to transport folded protein effectors via a periplasmic helical polymer called the endopilus, composed of one major and four minor ...Gram-negative bacteria employ the type II secretion system (T2SS) to transport folded protein effectors via a periplasmic helical polymer called the endopilus, composed of one major and four minor pilin subunits. Endopili resemble type IV pili but feature a conserved calcium-binding site stabilizing their major pilins. Endopilus polymerization is coupled to substrate translocation through a dedicated outer membrane channel. We compared T2SSs from plant and human pathogens, Dickeya dadantii and Klebsiella oxytoca, respectively. Despite different ecological niches and secreted effectors, their major pilins (OutG and PulG) share >77% sequence identity. Using NMR and cryo-EM, we solved structures of calcium-bound OutG monomer, as well as OutG and PulG endopili at 3.6 Å resolution. Combining structural, mutational, and biophysical analyses with in vivo assays, we identified key determinants of secretion specificity and endopilus stability. Our findings reveal how minor sequence variations in conserved nanomachines drive functional adaptation to diverse environments. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_75833.map.gz | 59.7 MB | EMDB map data format | |
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| Header (meta data) | emd-75833-v30.xml emd-75833.xml | 17.2 KB 17.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_75833_fsc.xml | 8.5 KB | Display | FSC data file |
| Images | emd_75833.png | 29.9 KB | ||
| Filedesc metadata | emd-75833.cif.gz | 5.5 KB | ||
| Others | emd_75833_additional_1.map.gz emd_75833_half_map_1.map.gz emd_75833_half_map_2.map.gz | 52.6 MB 59.3 MB 59.3 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-75833 ftp://data.pdbj.org/pub/emdb/structures/EMD-75833 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 11mfMC ![]() 11meC ![]() 29jdC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_75833.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: EMReady sharpned map
| File | emd_75833_additional_1.map | ||||||||||||
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| Annotation | EMReady sharpned map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_75833_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_75833_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : PulG T2SS filament
| Entire | Name: PulG T2SS filament |
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| Components |
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-Supramolecule #1: PulG T2SS filament
| Supramolecule | Name: PulG T2SS filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Klebsiella oxytoca (bacteria) |
-Macromolecule #1: Type II secretion system core protein G
| Macromolecule | Name: Type II secretion system core protein G / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: Klebsiella oxytoca (bacteria) |
| Molecular weight | Theoretical: 14.200957 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: FTLLEIMVVI VILGVLASLV VPNLMGNKEK ADRQKVVSDL VALEGALDMY KLDNSRYPTT EQGLQALVSA PSAEPHARNY PEGGYIRRL PQDPWGSDYQ LLSPGQHGQV DIFSLGPDGV PESNDDIGNW T UniProtKB: UNIPROTKB: A0ABF7PG33 |
-Macromolecule #2: CALCIUM ION
| Macromolecule | Name: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: CA |
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| Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Klebsiella oxytoca (bacteria)
Authors
United States, 1 items
Citation




Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

