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==Cryo-EM structure of the tail tip region of Parabacteroide phage PD491P1 (imposed with C3 symmetry)==
<StructureSection load='9wwc' size='340' side='right'caption='[[9wwc]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9wwc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Parabacteroides_phage_PD491P1 Parabacteroides phage PD491P1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WWC 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]] 4.5&#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=9wwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wwc OCA], [https://pdbe.org/9wwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wwc RCSB], [https://www.ebi.ac.uk/pdbsum/9wwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wwc ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Bacteriophages play crucial roles in modulating the human gut microbiome, yet structural characterization of prevalent gut phages remains limited. Here, we present high-resolution cryo-EM structures of Parabacteroides phage PD491P1, which is one of the most abundant bacteriophages in the human gut. The structures reveal its mature virion organization, including the capsid, head-to-tail interface, and tail tip regions. Strikingly, PD491P1 exhibits an exceptionally extensive disulfide bond network that covalently stabilizes nearly the entire virion. Unique structural features include an elaborate portal-adaptor-terminator interface and distinctive, upward-pointing and flexible tail fibers with multiple putative host recognition domains. These structural adaptations may enable phage PD491P1 to achieve survival and robust infection in the challenging gut environment. These findings expand our understanding of gut phage structural diversity, reveal mechanistic insights into phage stability and infection, and provide a foundation for future development of phage-based microbiome therapeutics.

Cryo-EM structures of prevalent gut phage PD491P1 uncover extensive disulfide stabilization and distinct structural adaptations.,Cai C, Wang A, Shao Q, Zhang J, Wang Y, Hu H, Yuan K, Li L, Wang X, Fang Q, Ma Y Structure. 2026 Jun 4;34(6):942-954.e2. doi: 10.1016/j.str.2026.04.005. Epub 2026 , May 4. PMID:42086047<ref>PMID:42086047</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Parabacteroides phage PD491P1]]
[[Category: Cai C]]
[[Category: Shao Q]]
[[Category: Wang A]]