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Yorodumi- EMDB-60903: Cryo-EM structure of the type I pilus from enterotoxigenic Escher... -
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Open data
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Basic information
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| Title | Cryo-EM structure of the type I pilus from enterotoxigenic Escherichia coli | |||||||||
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Keywords | Type 1 pili / FimA / CELL ADHESION | |||||||||
| Function / homology | Fimbrial-type adhesion domain / Fimbrial protein / : / Fimbrial-type adhesion domain superfamily / cell adhesion involved in single-species biofilm formation / Adhesion domain superfamily / pilus / FimA Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||
Authors | Kawahara K / Oki H / Nakamura S | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: Structure / Year: 2025Title: High-resolution cryo-EM analysis visualizes hydrated type I and IV pilus structures from enterotoxigenic Escherichia coli. Authors: Kazuki Kawahara / Hiroya Oki / Minato Iimori / Ryuki Muramoto / Tomoya Imai / Christoph Gerle / Hideki Shigematsu / Shigeaki Matsuda / Tetsuya Iida / Shota Nakamura / ![]() Abstract: Pathogenic bacteria utilize a variety of pilus filaments to colonize intestinal epithelia, including those synthesized by the chaperone-usher or type IV pilus assembly pathway. Despite the importance ...Pathogenic bacteria utilize a variety of pilus filaments to colonize intestinal epithelia, including those synthesized by the chaperone-usher or type IV pilus assembly pathway. Despite the importance of these filaments as potential drug and vaccine targets, their large size and dynamic nature make high-resolution structure determination challenging. Here, we used cryo-electron microscopy (cryo-EM) and whole-genome sequencing to determine the structures of type I and IV pili expressed in enterotoxigenic Escherichia coli. Well-defined cryo-EM maps at resolutions of 2.2 and 1.8 Å for type I and IV pilus, respectively, facilitated the de novo structural modeling for these filaments, revealing side-chain structures in detail. We resolved thousands of hydrated water molecules around and within the inner core of the filaments, which stabilize the otherwise metastable quaternary subunit assembly. The high-resolution structures offer novel insights into subunit-subunit interactions, and provide important clues to understand pilus assembly, stability, and flexibility. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_60903.map.gz | 122.9 MB | EMDB map data format | |
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| Header (meta data) | emd-60903-v30.xml emd-60903.xml | 17.7 KB 17.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_60903_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_60903.png | 72.2 KB | ||
| Masks | emd_60903_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-60903.cif.gz | 5.4 KB | ||
| Others | emd_60903_additional_1.map.gz emd_60903_half_map_1.map.gz emd_60903_half_map_2.map.gz | 230.2 MB 226.6 MB 226.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-60903 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-60903 | HTTPS FTP |
-Validation report
| Summary document | emd_60903_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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| Full document | emd_60903_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | emd_60903_validation.xml.gz | 21.7 KB | Display | |
| Data in CIF | emd_60903_validation.cif.gz | 27.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60903 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60903 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9iugMC ![]() 9iufC 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_60903.map.gz / Format: CCP4 / Size: 244.1 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: 0.752 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_60903_msk_1.map | ||||||||||||
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-Additional map: sharpening map
| File | emd_60903_additional_1.map | ||||||||||||
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| Annotation | sharpening map | ||||||||||||
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-Half map: #2
| File | emd_60903_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_60903_half_map_2.map | ||||||||||||
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Sample components
-Entire : Type-1 fimbrial protein FimA
| Entire | Name: Type-1 fimbrial protein FimA |
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| Components |
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-Supramolecule #1: Type-1 fimbrial protein FimA
| Supramolecule | Name: Type-1 fimbrial protein FimA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: FimA
| Macromolecule | Name: FimA / type: protein_or_peptide / ID: 1 / Number of copies: 21 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 16.363992 KDa |
| Sequence | String: ETTPTTVNGG TVHFKGEVVN AACAVDAGSV DQTVQLGQVR TASLKQTGAT SSAVGFNIQL NDCDTSVATK AAVAFLGTAI DSAHPKVLA LQSSAAGSAT NVGVQILDRT GAELTLDGAT FSVQTTLNNG TNTIPFRARY YAIGEATPGA ANADATFKVQ Y Q UniProtKB: FimA |
-Macromolecule #2: water
| Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 2846 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-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: 8 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV |
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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: 53.77 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: 1.6 µm / Nominal defocus min: 1.4000000000000001 µm |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9iug: |
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About Yorodumi



Keywords
Authors
Japan, 2 items
Citation


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FIELD EMISSION GUN
