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==Acinetobacter phage AP205==
<StructureSection load='8toc' size='340' side='right'caption='[[8toc]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8toc]] is a 181 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_phage_AP205 Acinetobacter phage AP205] and [https://en.wikipedia.org/wiki/Bacteria_abnormis Bacteria abnormis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TOC 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]] 3.11&#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=8toc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8toc OCA], [https://pdbe.org/8toc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8toc RCSB], [https://www.ebi.ac.uk/pdbsum/8toc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8toc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9AZ43_9VIRU Q9AZ43_9VIRU] 
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== Publication Abstract from PubMed ==
Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics.

Structural basis of Acinetobacter type IV pili targeting by an RNA virus.,Meng R, Xing Z, Chang JY, Yu Z, Thongchol J, Xiao W, Wang Y, Chamakura K, Zeng Z, Wang F, Young R, Zeng L, Zhang J Nat Commun. 2024 Mar 29;15(1):2746. doi: 10.1038/s41467-024-47119-5. PMID:38553443<ref>PMID:38553443</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8toc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Acinetobacter phage AP205]]
[[Category: Bacteria abnormis]]
[[Category: Large Structures]]
[[Category: Chang J]]
[[Category: Meng R]]
[[Category: Xing Z]]
[[Category: Zhang J]]