30ys: Difference between revisions
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Created page with "'''Unreleased structure''' The entry 30ys is ON HOLD Authors: Goulet, A., Cambillau, C. Description: Capsid of the Oenococcus oeni phage OE33PA Category: Unreleased Structures Category: Goulet, A Category: Cambillau, C" |
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==Capsid of the Oenococcus oeni phage OE33PA== | |||
<StructureSection load='30ys' size='340' side='right'caption='[[30ys]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[30ys]] is a 7 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=30YS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30YS 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]] 2.8Å</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=30ys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30ys OCA], [https://pdbe.org/30ys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30ys RCSB], [https://www.ebi.ac.uk/pdbsum/30ys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30ys 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 30ys" style="background-color:#fffaf0;"></div> | ||
[[Category: Cambillau | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oenococcus phage phiOE33PA]] | |||
[[Category: Cambillau C]] | |||
[[Category: Goulet A]] | |||
