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| Title | Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum. |
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| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 3257, Year 2025 |
| Publish date | Apr 5, 2025 |
 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 /      |
| PubMed 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. |
 External links | Nat Commun / PubMed:40188083 / PubMed Central |
| Methods | EM (single particle) / EM (helical sym.) |
| Resolution | 3.11 - 12.7 Å |
| Structure data | EMDB-45419, PDB-9cb9: EMDB-45420, PDB-9cba: EMDB-45435, PDB-9cc7:  EMDB-45436: PhiTE C6 connector reconstruction  EMDB-45439: PhiTE C12 connector reconstruction  EMDB-45486: Reconstruction of PhiTE baseplate with C6 symmetry imposed  EMDB-45487: Bacteriophage PhiTE baseplate with C3 symmetry imposed  EMDB-45488: Bacteriophage PhiTE baseplate locally refined reconstruction with C6 symmetry imposed (particle subtraction and deep EM enhancing performed)  EMDB-45491: Bacteriophage PhiTE baseplate reconstruction with C6 symmetry imposed  EMDB-45613: Bacteriophage PhiTE full tail reconstruction with C3 symmetry imposed EMDB-45937, PDB-9cul: EMDB-45953, PDB-9cuy: EMDB-48317, PDB-9mjn: |
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 Keywords | VIRAL PROTEIN / Tail / Sheath / Tube / PhiTE / Virus / Phage / connector / neck / adaptor / tail terminator / head completion / portal / capsid / head / MCP / decoration / icosahedral / baseplate / sheath initiator / tube initiator / hub / puncture apparatus / fibers / wedge / tape measure protein |
pectobacterium phage phite (virus)