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Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB...
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| Published in: | Nature communications 2025-02, Vol.16 (1), p.1695, Article 1695 |
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| creator | Gu, Zhiwei Ge, Xiaofei Wang, Jiawei |
| description | F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB from
Listeria monocytogenes
. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies.
F-type phage-tail like bacteriocins (PTLBs) are protein complexes with bactericidal activity and share similarity with non-contractile phage tails. Here, authors report the atomic structure of monocin, an F-type PTLB from listeria monocytogenes. |
| doi_str_mv | 10.1038/s41467-025-57075-3 |
| format | article |
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Listeria monocytogenes
. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies.
F-type phage-tail like bacteriocins (PTLBs) are protein complexes with bactericidal activity and share similarity with non-contractile phage tails. Here, authors report the atomic structure of monocin, an F-type PTLB from listeria monocytogenes.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/s41467-025-57075-3</identifier><identifier>PMID: 39956822</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/28 ; 631/326/596/432 ; 631/45/535 ; 631/535/1258/1259 ; 631/57/2272 ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Atomic properties ; Atomic structure ; Bactericidal activity ; Bacteriocins ; Bacteriocins - chemistry ; Bacteriocins - metabolism ; Bacteriocins - pharmacology ; Bacteriophages - genetics ; Bacteriophages - metabolism ; Cell death ; Contractility ; Crystallography, X-Ray ; Genetic engineering ; Humanities and Social Sciences ; Listeria ; Listeria monocytogenes ; Listeria monocytogenes - drug effects ; Listeria monocytogenes - virology ; Models, Molecular ; Molecular structure ; multidisciplinary ; Phages ; Protein structure ; Proteins ; Science ; Science (multidisciplinary) ; Viral Tail Proteins - chemistry ; Viral Tail Proteins - genetics ; Viral Tail Proteins - metabolism</subject><ispartof>Nature communications, 2025-02, Vol.16 (1), p.1695, Article 1695</ispartof><rights>The Author(s) 2025</rights><rights>2025. The Author(s).</rights><rights>Copyright Nature Publishing Group 2025</rights><rights>The Author(s) 2025 2025</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c2273-d61d97b73f6337342a3506e61a58b20a11afc776ea765791a0c92299bba0e29e3</cites><orcidid>0009-0005-9626-7061 ; 0000-0001-9893-8539 ; 0009-0006-5573-5022</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/3167421169/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/3167421169?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768,75096</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39956822$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gu, Zhiwei</creatorcontrib><creatorcontrib>Ge, Xiaofei</creatorcontrib><creatorcontrib>Wang, Jiawei</creatorcontrib><title>Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB from
Listeria monocytogenes
. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies.
F-type phage-tail like bacteriocins (PTLBs) are protein complexes with bactericidal activity and share similarity with non-contractile phage tails. Here, authors report the atomic structure of monocin, an F-type PTLB from listeria monocytogenes.</description><subject>101/28</subject><subject>631/326/596/432</subject><subject>631/45/535</subject><subject>631/535/1258/1259</subject><subject>631/57/2272</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Atomic properties</subject><subject>Atomic structure</subject><subject>Bactericidal activity</subject><subject>Bacteriocins</subject><subject>Bacteriocins - chemistry</subject><subject>Bacteriocins - metabolism</subject><subject>Bacteriocins - pharmacology</subject><subject>Bacteriophages - genetics</subject><subject>Bacteriophages - metabolism</subject><subject>Cell death</subject><subject>Contractility</subject><subject>Crystallography, X-Ray</subject><subject>Genetic engineering</subject><subject>Humanities and Social Sciences</subject><subject>Listeria</subject><subject>Listeria monocytogenes</subject><subject>Listeria monocytogenes - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gu, Zhiwei</au><au>Ge, Xiaofei</au><au>Wang, Jiawei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2025-02-16</date><risdate>2025</risdate><volume>16</volume><issue>1</issue><spage>1695</spage><pages>1695-</pages><artnum>1695</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB from
Listeria monocytogenes
. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies.
F-type phage-tail like bacteriocins (PTLBs) are protein complexes with bactericidal activity and share similarity with non-contractile phage tails. Here, authors report the atomic structure of monocin, an F-type PTLB from listeria monocytogenes.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>39956822</pmid><doi>10.1038/s41467-025-57075-3</doi><orcidid>https://orcid.org/0009-0005-9626-7061</orcidid><orcidid>https://orcid.org/0000-0001-9893-8539</orcidid><orcidid>https://orcid.org/0009-0006-5573-5022</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Publicly Available Content Database; Springer Nature - Connect here FIRST to enable access; PubMed Central; Springer Nature - nature.com Journals - Fully Open Access |
| subjects | 101/28 631/326/596/432 631/45/535 631/535/1258/1259 631/57/2272 Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Atomic properties Atomic structure Bactericidal activity Bacteriocins Bacteriocins - chemistry Bacteriocins - metabolism Bacteriocins - pharmacology Bacteriophages - genetics Bacteriophages - metabolism Cell death Contractility Crystallography, X-Ray Genetic engineering Humanities and Social Sciences Listeria Listeria monocytogenes Listeria monocytogenes - drug effects Listeria monocytogenes - virology Models, Molecular Molecular structure multidisciplinary Phages Protein structure Proteins Science Science (multidisciplinary) Viral Tail Proteins - chemistry Viral Tail Proteins - genetics Viral Tail Proteins - metabolism |
| title | Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes |
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