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dc.contributor.authorPiper, Sarah J
dc.contributor.authorBrillault, Lou
dc.contributor.authorRothnagel, Rosalba
dc.contributor.authorCroll, Tristan
dc.contributor.authorBox, Joseph K
dc.contributor.authorChassagnon, Irene
dc.contributor.authorScherer, Sebastian
dc.contributor.authorGoldie, Kenneth N
dc.contributor.authorJones, Sandra A
dc.contributor.authorSchepers, Femke
dc.contributor.authorHartley-Tassell, Lauren
dc.contributor.authorVe, Thomas
dc.contributor.authorBusby, Jason N
dc.contributor.authorDalziel, Julie E
dc.contributor.authorLott, J Shaun
dc.contributor.authorHankamer, Ben
dc.contributor.authorStahlberg, Henning
dc.contributor.authorHurst, Mark RH
dc.contributor.authorLandsberg, Michael J
dc.date.accessioned2019-07-05T05:10:45Z
dc.date.available2019-07-05T05:10:45Z
dc.date.issued2019
dc.identifier.issn2041-1723
dc.identifier.doi10.1038/s41467-019-09890-8
dc.identifier.urihttp://hdl.handle.net/10072/386196
dc.description.abstractABC toxins are pore-forming virulence factors produced by pathogenic bacteria. YenTcA is the pore-forming and membrane binding A subunit of the ABC toxin YenTc, produced by the insect pathogen Yersinia entomophaga. Here we present cryo-EM structures of YenTcA, purified from the native source. The soluble pre-pore structure, determined at an average resolution of 4.4 Å, reveals a pentameric assembly that in contrast to other characterised ABC toxins is formed by two TcA-like proteins (YenA1 and YenA2) and decorated by two endochitinases (Chi1 and Chi2). We also identify conformational changes that accompany membrane pore formation by visualising YenTcA inserted into liposomes. A clear outward rotation of the Chi1 subunits allows for access of the protruding translocation pore to the membrane. Our results highlight structural and functional diversity within the ABC toxin subfamily, explaining how different ABC toxins are capable of recognising diverse hosts.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.relation.ispartofpagefrom1
dc.relation.ispartofpageto12
dc.relation.ispartofissue1
dc.relation.ispartofjournalNature Communications
dc.relation.ispartofvolume10
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode11
dc.titleCryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
gro.rights.copyright© 2019 Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
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gro.griffith.authorVe, Thomas
gro.griffith.authorHartley-Tassell, Lauren E.


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