{"type":"journal_article","author":[{"full_name":"Bräuning, Bastian","first_name":"Bastian","last_name":"Bräuning"},{"last_name":"Bertosin","first_name":"Eva","full_name":"Bertosin, Eva"},{"full_name":"Praetorius, Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","first_name":"Florian M","last_name":"Praetorius"},{"full_name":"Ihling, Christian","first_name":"Christian","last_name":"Ihling"},{"full_name":"Schatt, Alexandra","last_name":"Schatt","first_name":"Alexandra"},{"first_name":"Agnes","last_name":"Adler","full_name":"Adler, Agnes"},{"first_name":"Klaus","last_name":"Richter","full_name":"Richter, Klaus"},{"first_name":"Andrea","last_name":"Sinz","full_name":"Sinz, Andrea"},{"full_name":"Dietz, Hendrik","first_name":"Hendrik","last_name":"Dietz"},{"first_name":"Michael","last_name":"Groll","full_name":"Groll, Michael"}],"article_processing_charge":"No","external_id":{"pmid":["29728606"]},"article_type":"original","language":[{"iso":"eng"}],"status":"public","doi":"10.1038/s41467-018-04139-2","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","day":"04","volume":9,"pmid":1,"month":"05","extern":"1","citation":{"apa":"Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>","ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","ista":"Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.","ama":"Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>","chicago":"Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>.","mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","short":"B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018)."},"oa_version":"Published Version","_id":"14284","publisher":"Springer Nature","intvolume":"         9","publication_status":"published","oa":1,"date_updated":"2023-11-07T11:46:12Z","publication_identifier":{"issn":["2041-1723"]},"scopus_import":"1","year":"2018","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"publication":"Nature Communications","article_number":"1806","quality_controlled":"1","abstract":[{"lang":"eng","text":"Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2023-09-06T12:07:33Z","date_published":"2018-05-04T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}]}