8tob: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8tob is ON HOLD
+==Acinetobacter GP16 Type IV pilus==
+<StructureSection load='8tob' size='340' side='right'caption='[[8tob]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8tob]] is a 44 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_higginsii Acinetobacter higginsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TOB 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]] 3.14&#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=8tob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tob OCA], [https://pdbe.org/8tob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tob RCSB], [https://www.ebi.ac.uk/pdbsum/8tob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tob ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/N9RQW9_9GAMM N9RQW9_9GAMM]
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Meng, R., Xing, Z., Zhang, J.
+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>
-Description: Acinetobacter GP16 Type IV pilus
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Xing, Z]]
+<div class="pdbe-citations 8tob" style="background-color:#fffaf0;"></div>
-[[Category: Zhang, J]]
+== References ==
-[[Category: Meng, R]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Acinetobacter higginsii]]
+[[Category: Large Structures]]
+[[Category: Meng R]]
+[[Category: Xing Z]]
+[[Category: Zhang J]]