8bfp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8bfp is ON HOLD Authors: Ouyang, R. Description: Jumbo Phage phi-kp24 empty capsid pentamer hexamers Category: Unreleased Structures [[Category...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Jumbo Phage phi-kp24 empty capsid pentamer hexamers== | |
| + | <StructureSection load='8bfp' size='340' side='right'caption='[[8bfp]], [[Resolution|resolution]] 4.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8bfp]] is a 35 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_phage_vB_KpM_FBKp24 Klebsiella phage vB_KpM_FBKp24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BFP 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]] 4.1Å</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=8bfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bfp OCA], [https://pdbe.org/8bfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bfp RCSB], [https://www.ebi.ac.uk/pdbsum/8bfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bfp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7U0GBA8_9CAUD A0A7U0GBA8_9CAUD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Klebsiella jumbo myophage varphiKp24 displays an unusually complex arrangement of tail fibers interacting with a host cell. In this study, we combine cryo-electron microscopy methods, protein structure prediction methods, molecular simulations, microbiological and machine learning approaches to explore the capsid, tail, and tail fibers of varphiKp24. We determine the structure of the capsid and tail at 4.1 A and 3.0 A resolution. We observe the tail fibers are branched and rearranged dramatically upon cell surface attachment. This complex configuration involves fourteen putative tail fibers with depolymerase activity that provide varphiKp24 with the ability to infect a broad panel of capsular polysaccharide (CPS) types of Klebsiella pneumoniae. Our study provides structural and functional insight into how varphiKp24 adapts to the variable surfaces of capsulated bacterial pathogens, which is useful for the development of phage therapy approaches against pan-drug resistant K. pneumoniae strains. | ||
| - | + | High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers.,Ouyang R, Costa AR, Cassidy CK, Otwinowska A, Williams VCJ, Latka A, Stansfeld PJ, Drulis-Kawa Z, Briers Y, Pelt DM, Brouns SJJ, Briegel A Nat Commun. 2022 Nov 24;13(1):7241. doi: 10.1038/s41467-022-34972-5. PMID:36433970<ref>PMID:36433970</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Ouyang | + | <div class="pdbe-citations 8bfp" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Klebsiella phage vB_KpM_FBKp24]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ouyang R]] | ||
Current revision
Jumbo Phage phi-kp24 empty capsid pentamer hexamers
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