9osb: Difference between revisions

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'''Unreleased structure'''


The entry 9osb is ON HOLD
==D3 prohead 1==
<StructureSection load='9osb' size='340' side='right'caption='[[9osb]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9osb]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_D3 Pseudomonas phage D3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OSB 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]] 3.5&#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=9osb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9osb OCA], [https://pdbe.org/9osb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9osb RCSB], [https://www.ebi.ac.uk/pdbsum/9osb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9osb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tailed bacteriophages comprise the largest structural family of viruses with close relatives in archaea and the eukaryotic herpesviruses. The common assembly pathway produces an icosahedrally symmetric protein shell, called capsid, into which the double-stranded DNA genome is packaged. While capsid sizes and amino acid sequences vary considerably, the major capsid protein (MCP) folds are remarkably similar throughout the family. To investigate the mechanisms governing capsid size, we characterize the procapsid and mature capsid of phage D3, which expresses an icosahedral lattice with Triangulation number T = 9. We find that the MCP scaffold domain binds to the interior capsid surface, acting as a clamp to constrain subunit interactions. Following scaffold digestion, the MCP capsid domains form strong interactions that maintain capsid structure throughout maturation. The scaffold constraints appear critical for capsid size determination and provide important understanding of the factors governing capsid assembly in general and expands our understanding of these ecologically and biomedically important viruses.


Authors:  
Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid.,Belford AK, Maurer JB, Duda RL, Huet A, Conway JF Nat Commun. 2025 Nov 23;16(1):11586. doi: 10.1038/s41467-025-66648-1. PMID:41274907<ref>PMID:41274907</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 9osb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage D3]]
[[Category: Belford AK]]
[[Category: Conway JF]]
[[Category: Duda RL]]
[[Category: Huet A]]
[[Category: Maurer JB]]
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