View source for 30yw


==Stopper and tail terminator assembly of the phage OE33PA==
<StructureSection load='30yw' size='340' side='right'caption='[[30yw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[30yw]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Oenococcus_phage_phiOE33PA Oenococcus phage phiOE33PA]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=30YW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30YW 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]] 2.8&#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=30yw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30yw OCA], [https://pdbe.org/30yw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30yw RCSB], [https://www.ebi.ac.uk/pdbsum/30yw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30yw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we report cryo-electron microscopy structures of the Oenococcus oeni siphophage OE33PA, providing the first atomic resolution view of a phage infecting this bacterium important for the wine industry. While the overall virion architecture is conserved, the adhesion device displays distinctive features. Its receptor-binding proteins adopt multiple orientations, revealing an intrinsically dynamic assembly. In situ cryo-electron tomography captures distinct conformations upon host attachment, providing rare structural insight into interactions with Gram-positive hosts. Additionally, functional assays show that a highly mobile carbohydrate-binding module in the distal tail protein mediates host-specific binding. Furthermore, the tape measure protein, central to phage assembly and infectivity, adopts a hexameric organization, updating the prevailing trimeric model in siphophages. Together, these findings reveal a dynamic adhesion device in a phage infecting Gram-positive bacteria and highlight the structural and functional diversity of phages.

Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.,Schmitt L, Chaib A, Ptchelkine D, Kandiah E, Le Marrec C, Cambillau C, Goulet A bioRxiv [Preprint]. 2026 May 25:2026.05.20.726473. doi: , 10.64898/2026.05.20.726473. PMID:42244550<ref>PMID:42244550</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Oenococcus phage phiOE33PA]]
[[Category: Cambillau C]]
[[Category: Goulet A]]