View source for 9mjn


==Near complete virion structure of bacteriophage PhiTE==
<StructureSection load='9mjn' size='340' side='right'caption='[[9mjn]], [[Resolution|resolution]] 12.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9mjn]] is a 1939 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_phage_phiTE Pectobacterium phage phiTE]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MJN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 12.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9mjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mjn OCA], [https://pdbe.org/9mjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mjn RCSB], [https://www.ebi.ac.uk/pdbsum/9mjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mjn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K9L587_9CAUD K9L587_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 phiTE 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 phiTE, 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.

Global structural survey of the flagellotropic myophage phiTE infecting agricultural pathogen Pectobacterium atrosepticum.,Hodgkinson-Bean J, Ayala R, Jayawardena N, Rutter GL, Watson BNJ, Mayo-Munoz D, Keal J, Fineran PC, Wolf M, Bostina M Nat Commun. 2025 Apr 5;16(1):3257. doi: 10.1038/s41467-025-58514-x. PMID:40188083<ref>PMID:40188083</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9mjn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pectobacterium phage phiTE]]
[[Category: Ayala R]]
[[Category: Hodgkinson-Bean J]]