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Yorodumi- EMDB-52523: CryoEM structure of F-ENA fibers on the spores of Bacillus thurin... -
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Open data
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Basic information
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| Title | CryoEM structure of F-ENA fibers on the spores of Bacillus thuringiensis serovar kurstaki | |||||||||
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Keywords | ENA / endospore appendage / protein fiber / helical / PROTEIN FIBRIL | |||||||||
| Function / homology | : Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.23 Å | |||||||||
Authors | Sleutel M / Remaut H | |||||||||
| Funding support | Belgium, 1 items
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Citation | Journal: bioRxiv / Year: 2025Title: Cryo-EM analysis of the extrasporal matrix identifies F-ENA as a widespread family of endospore appendages across the Firmicutes phylum. Authors: Mike Sleutel / Adrià Sogues / Nani Van Gerven / Unni Lise Jonsmoen / Inge Van Molle / Marcus Fislage / Laurent Dirk Theunissen / Nathan F Bellis / Diana P Baquero / Edward H Egelman / Mart ...Authors: Mike Sleutel / Adrià Sogues / Nani Van Gerven / Unni Lise Jonsmoen / Inge Van Molle / Marcus Fislage / Laurent Dirk Theunissen / Nathan F Bellis / Diana P Baquero / Edward H Egelman / Mart Krupovic / Fengbin Wang / Marina Aspholm / Han Remaut / ![]() Abstract: For over 100 years, (Bt) has been used as an agricultural biopesticide to control pests caused by insect species in the orders of Lepidoptera, Diptera and Coleoptera. Under nutrient starvation, Bt ...For over 100 years, (Bt) has been used as an agricultural biopesticide to control pests caused by insect species in the orders of Lepidoptera, Diptera and Coleoptera. Under nutrient starvation, Bt cells differentiate into spores and associated toxin crystals that can adopt biofilm-like aggregates. We reveal that such Bt spore/toxin biofilms are embedded in a fibrous extrasporal matrix (ESM), and using cryoID, we resolved the structure and molecular identity of an uncharacterized type of pili, referred to here as Fibrillar ENdospore Appendages or 'F-ENA'. F-ENA are monomolecular protein polymers tethered to the exosporium of Bt and are decorated with a flexible tip fibrillum. Phylogenetic analysis reveals that F-ENA is widespread not only in the class Bacilli, but also in the class Clostridia, and the cryoEM structures of F-ENA filaments from and reveal subunits with a generic head-neck domain structure, where the β-barrel neck of variable length latch onto a preceding head domain through short N-terminal hook peptides. In , two collagen-like proteins (CLP) respectively tether F-ENA to the exosporium (F-Anchor), or constitute the tip fibrillum at the distal terminus of F-ENA (F-BclA). Sedimentation assays point towards F-ENA involvement in spore-spore clustering, likely mediated via F-BclA contacts and F-ENA bundling through the antiparallel interlocking of the head-neck units. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_52523.map.gz | 3.2 MB | EMDB map data format | |
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| Header (meta data) | emd-52523-v30.xml emd-52523.xml | 21.5 KB 21.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_52523_fsc.xml | 8.4 KB | Display | FSC data file |
| Images | emd_52523.png | 76.8 KB | ||
| Masks | emd_52523_msk_1.map | 64 MB | Mask map | |
| Filedesc metadata | emd-52523.cif.gz | 6 KB | ||
| Others | emd_52523_additional_1.map.gz emd_52523_half_map_1.map.gz emd_52523_half_map_2.map.gz | 3.2 MB 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52523 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52523 | HTTPS FTP |
-Validation report
| Summary document | emd_52523_validation.pdf.gz | 677.3 KB | Display | EMDB validaton report |
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| Full document | emd_52523_full_validation.pdf.gz | 676.8 KB | Display | |
| Data in XML | emd_52523_validation.xml.gz | 16.4 KB | Display | |
| Data in CIF | emd_52523_validation.cif.gz | 21.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52523 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52523 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9hzeMC ![]() 9i65C ![]() 9n0bC 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_52523.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: 1.39 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_52523_msk_1.map | ||||||||||||
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-Additional map: #1
| File | emd_52523_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_52523_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_52523_half_map_2.map | ||||||||||||
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Sample components
-Entire : F-ENA
| Entire | Name: F-ENA |
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| Components |
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-Supramolecule #1: F-ENA
| Supramolecule | Name: F-ENA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 8.627 kDa/nm |
-Macromolecule #1: DUF4183 domain-containing protein
| Macromolecule | Name: DUF4183 domain-containing protein / type: protein_or_peptide / ID: 1 / Number of copies: 24 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 9.692923 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MPIIQPFMAS RRFTSTLGAG TGTGAAFAIA ATACLNDAGT TATAFPTFTY YNLYVNGILQ PSVNSSVTTG PTGAITIPGG DALDGGIPI TIEFIVT UniProtKB: UNIPROTKB: A0AAX0C6N4 |
-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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| Grid | Model: Quantifoil R2/1 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | JEOL CRYO ARM 300 |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9hze: |
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Keywords
Authors
Belgium, 1 items
Citation






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FIELD EMISSION GUN
