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Open data
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Basic information
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Title | Near complete virion structure of bacteriophage PhiTE | |||||||||
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![]() | Tail / Sheath / Tube / PhiTE / Virus / Phage | |||||||||
Function / homology | ![]() virus tail, fiber / viral tail assembly / host cell cytoplasm / virion attachment to host cell Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 12.7 Å | |||||||||
![]() | Hodgkinson-Bean J / Ayala R | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum. Authors: James Hodgkinson-Bean / Rafael Ayala / Nadishka Jayawardena / Georgia L Rutter / Bridget N J Watson / David Mayo-Muñoz / James Keal / Peter C Fineran / Matthias Wolf / Mihnea Bostina / ![]() ![]() ![]() ![]() ![]() Abstract: Bacteriophages offer a promising alternative to drug-based treatments due to their effectiveness and host specificity. This is particularly important in agriculture as a biocontrol agent of plant ...Bacteriophages offer a promising alternative to drug-based treatments due to their effectiveness and host specificity. This is particularly important in agriculture as a biocontrol agent of plant diseases. Phage engineering is facilitated by structural knowledge. However, structural information regarding bacteriophages infecting plant pathogens is limited. Here, we present the cryo-EM structure of bacteriophage φTE that infects plant pathogen Pectobacterium atrosepticum. The structure reveals a distinct neck topology compared with other myophages, where tail terminator proteins compensate for reduced connectivity between sheath subunits. A contact network between tail fibers, the sheath initiator, and baseplate wedge proteins provides insights into triggers that transduce conformational changes from the baseplate to the sheath to orchestrate contraction. We observe two distinct oligomeric states of the tape measure protein (TMP), which is six-fold in regions proximal to the N-terminus and throughout most of the tail, while three-fold at the C-terminus, indicating that the TMP may be proteolytically cleaved. Our results provide a structural atlas of the model bacteriophage φTE, enhancing future interpretation of phage host interactions in pectobacteria. We anticipate that our structure will inform rational design of biocontrol agents against plant pathogens that cause diseases such as soft rot and blackleg disease in potatoes. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 303.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 37 KB 37 KB | Display Display | ![]() |
Images | ![]() | 51.5 KB | ||
Filedesc metadata | ![]() | 10.3 KB | ||
Others | ![]() ![]() ![]() | 241.4 MB 9.4 MB 9.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9mjnMC ![]() 9cb9C ![]() 9cbaC ![]() 9cc7C ![]() 9culC ![]() 9cuyC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 6.3045 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
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-Half map: #1
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Density Histograms |
-Half map: #2
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Density Histograms |
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Sample components
+Entire : Pectobacterium phage phiTE
+Supramolecule #1: Pectobacterium phage phiTE
+Macromolecule #1: Portal protein
+Macromolecule #2: PhiTE adaptor protein
+Macromolecule #3: PhiTE head completion protein
+Macromolecule #4: PhiTE tail terminator protein
+Macromolecule #5: Structural protein
+Macromolecule #6: Tail sheath protein
+Macromolecule #7: Head stabilization/decoration protein
+Macromolecule #8: Major capsid protein
+Macromolecule #9: Putative tail fiber protein
+Macromolecule #10: Sheath initiator protein
+Macromolecule #11: Dit-like phage tail protein N-terminal domain-containing protein
+Macromolecule #12: Cyanophage baseplate Pam3 plug gp18 domain-containing protein
+Macromolecule #13: Wedge 1 protein
+Macromolecule #14: baseplate assembly protein
+Macromolecule #15: Putative tape measure protein
+Macromolecule #16: Tail protein
+Macromolecule #17: Putative baseplate assembly protein
+Macromolecule #18: Short tail fiber
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 4 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER / Details: Ab initio helical model generated in cryoSPARC |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 12.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 12638 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |