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'''Unreleased structure'''


The entry 9wwa is ON HOLD
==Cryo-EM Structure of Parabacteroide phage PD491P1 head-to-tail interface==
<StructureSection load='9wwa' size='340' side='right'caption='[[9wwa]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9wwa]] is a 7 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=9WWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WWA 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]] 3.2&#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=9wwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wwa OCA], [https://pdbe.org/9wwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wwa RCSB], [https://www.ebi.ac.uk/pdbsum/9wwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wwa ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9wwa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parabacteroides phage PD491P1]]
[[Category: Cai C]]
[[Category: Shao Q]]
[[Category: Wang A]]
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