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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A2K8IA62_9CAUD A0A2K8IA62_9CAUD] | | [https://www.uniprot.org/uniprot/A0A2K8IA62_9CAUD A0A2K8IA62_9CAUD] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| E217 is a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Here, we describe the structure of the whole E217 virion before and after DNA ejection at 3.1 A and 4.5 A resolution, respectively, determined using cryogenic electron microscopy (cryo-EM). We identify and build de novo structures for 19 unique E217 gene products, resolve the tail genome-ejection machine in both extended and contracted states, and decipher the complete architecture of the baseplate formed by 66 polypeptide chains. We also determine that E217 recognizes the host O-antigen as a receptor, and we resolve the N-terminal portion of the O-antigen-binding tail fiber. We propose that E217 design principles presented in this paper are conserved across PB1-like Myoviridae phages of the Pbunavirus genus that encode a ~1.4 MDa baseplate, dramatically smaller than the coliphage T4.
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| High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217.,Li F, Hou CD, Lokareddy RK, Yang R, Forti F, Briani F, Cingolani G Nat Commun. 2023 Jul 8;14(1):4052. doi: 10.1038/s41467-023-39756-z. PMID:37422479<ref>PMID:37422479</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8env" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
