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Yorodumi- EMDB-18593: CryoEM structure of the type IV pilin PilA5 from Thermus thermophilus -
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Open data
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Basic information
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| Title | CryoEM structure of the type IV pilin PilA5 from Thermus thermophilus | |||||||||
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Keywords | Type IV pilin glycosylation / twitching motility / PROTEIN FIBRIL | |||||||||
| Function / homology | Prokaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like / cell outer membrane / periplasmic space / plasma membrane / Type IV narrow pilus major component PilA5 Function and homology information | |||||||||
| Biological species | ![]() Thermus thermophilus HB27 (bacteria) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 2.63 Å | |||||||||
Authors | Gold VAM / Neuhaus A / Gaines M / Isupov M / McLaren M | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: Commun Biol / Year: 2026Title: Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili. Authors: Alexander Neuhaus / Mathew McLaren / Michail N Isupov / Matthew Gaines / Emma Buzzard / Mateusz Sikora / Cyril Hanus / Bertram Daum / Beate Averhoff / Vicki A M Gold / ![]() Abstract: Type IV pili are long, filamentous structures that extend from bacterial cell surfaces, enabling cells to respond to changing environments and facilitating genome plasticity. Thermus thermophilus ...Type IV pili are long, filamentous structures that extend from bacterial cell surfaces, enabling cells to respond to changing environments and facilitating genome plasticity. Thermus thermophilus HB27 produces two different type IV pili, each exhibiting distinct structural and functional properties. Here, we combine cryo-electron tomography, mutagenesis, and AlphaFold predictions to generate hypothetical in situ models of the T. thermophilus type IV pilus assembly machinery. Using single-particle cryo-electron microscopy, we determine structures of both filament types, enabling modelling of their surface glycans. Molecular dynamics simulations further reveal the flexibility of these glycans on extrusion. Integration of the filament structures with our hypothetical model of the assembly machinery offers a framework for further dissecting T4P architecture and biogenesis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_18593.map.gz | 213.9 MB | EMDB map data format | |
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| Header (meta data) | emd-18593-v30.xml emd-18593.xml | 19.1 KB 19.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_18593_fsc.xml | 16.8 KB | Display | FSC data file |
| Images | emd_18593.png | 32 KB | ||
| Filedesc metadata | emd-18593.cif.gz | 6.3 KB | ||
| Others | emd_18593_half_map_1.map.gz emd_18593_half_map_2.map.gz | 475.6 MB 475.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18593 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18593 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8qqjMC ![]() 8qqdC 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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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_18593.map.gz / Format: CCP4 / Size: 512 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: 1.048 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_18593_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_18593_half_map_2.map | ||||||||||||
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Sample components
-Entire : Thermus thermophilus wide pilus
| Entire | Name: Thermus thermophilus wide pilus |
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| Components |
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-Supramolecule #1: Thermus thermophilus wide pilus
| Supramolecule | Name: Thermus thermophilus wide pilus / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() Thermus thermophilus HB27 (bacteria) |
-Macromolecule #1: Type IV narrow pilus major component PilA5
| Macromolecule | Name: Type IV narrow pilus major component PilA5 / type: protein_or_peptide / ID: 1 / Number of copies: 31 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Thermus thermophilus HB27 (bacteria) |
| Molecular weight | Theoretical: 11.441797 KDa |
| Sequence | String: FTLIELAIVI VIIGILVAIA VPRFVDLTDQ ANQANVDATA AAVRSAYAIA TVQAKGIPTC DQVFANLEGG STSGSTWTSS DNSTTVSCN ASADTFTISR GGKTRTLNLT VN UniProtKB: Type IV narrow pilus major component PilA5 |
-Macromolecule #3: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 31 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 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: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Digitization - Frames/image: 1-40 / Number real images: 2455 / Average electron dose: 47.6 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: 4.0 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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| Output model | ![]() PDB-8qqj: |
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About Yorodumi



Keywords
Thermus thermophilus HB27 (bacteria)
Authors
United Kingdom, 1 items
Citation









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FIELD EMISSION GUN

