View source for 9oee


==S. griseus TUA bound UmbA4 complexes==
<StructureSection load='9oee' size='340' side='right'caption='[[9oee]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9oee]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OEE 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]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1CAY:2,3-diacetamido-2,3-dideoxy-beta-D-mannopyranuronic+acid'>A1CAY</scene>, <scene name='pdbligand=A1CAZ:2,3-diacetamido-4-O-acetyl-2,3-dideoxy-beta-D-mannopyranuronic+acid'>A1CAZ</scene>, <scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene></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=9oee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oee OCA], [https://pdbe.org/9oee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oee RCSB], [https://www.ebi.ac.uk/pdbsum/9oee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oee ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93J50_STRCO Q93J50_STRCO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria exist in competitive and rapidly changing environments in which the nature of future threats cannot be easily predicted. Streptomyces coelicolor produces three antibacterial umbrella particles that harbor distinct polymorphic toxin domains and an overlapping set of six diversified lectins. Here, we show that the exquisite specificity of umbrella particles derives from lectin-mediated species-specific binding to previously undescribed hypervariable surface glycoconjugates. A cryo-electron microscopy (cryo-EM) structure of one such lectin in complex with its oligosaccharide substrate defines the molecular basis for targeting through the coordinated recognition of multiple glycan features. Biochemical and genetic studies of several target species, in conjunction with lectin-swapping experiments, support a model whereby S. coelicolor umbrella toxin diversification at the levels of lectin composition and toxin polymorphism represents a unique, two-tiered bet-hedging strategy. Bioinformatic analyses support this as a means by which the unusual architecture of umbrella toxins offers Streptomyces a generalizable strategy to antagonize an unpredictable array of competitors.

The unique architecture of umbrella toxins permits a two-tiered molecular bet-hedging strategy for interbacterial antagonism.,Zhao Q, Vlach J, Park YJ, Tan Y, Bertolli SK, Srinivas P, Liao P, Fitzpatrick CR, Dangl JL, Azadi P, DiMaio F, Peterson SB, Zhang D, Veesler D, Mougous JD Cell. 2025 Dec 2:S0092-8674(25)01249-8. doi: 10.1016/j.cell.2025.10.044. PMID:41338195<ref>PMID:41338195</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9oee" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces coelicolor]]
[[Category: DiMaio F]]
[[Category: Mougous JD]]
[[Category: Park YJ]]
[[Category: Veesler D]]
[[Category: Zhao Q]]