{"author":[{"full_name":"Bräuning, Bastian","first_name":"Bastian","last_name":"Bräuning"},{"first_name":"Eva","last_name":"Bertosin","full_name":"Bertosin, Eva"},{"full_name":"Praetorius, Florian M","last_name":"Praetorius","first_name":"Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62"},{"first_name":"Christian","last_name":"Ihling","full_name":"Ihling, Christian"},{"first_name":"Alexandra","last_name":"Schatt","full_name":"Schatt, Alexandra"},{"last_name":"Adler","first_name":"Agnes","full_name":"Adler, Agnes"},{"first_name":"Klaus","last_name":"Richter","full_name":"Richter, Klaus"},{"last_name":"Sinz","first_name":"Andrea","full_name":"Sinz, Andrea"},{"last_name":"Dietz","first_name":"Hendrik","full_name":"Dietz, Hendrik"},{"first_name":"Michael","last_name":"Groll","full_name":"Groll, Michael"}],"_id":"14284","main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"publication_identifier":{"issn":["2041-1723"]},"type":"journal_article","date_published":"2018-05-04T00:00:00Z","month":"05","publication":"Nature Communications","status":"public","publisher":"Springer Nature","extern":"1","year":"2018","language":[{"iso":"eng"}],"date_updated":"2023-11-07T11:46:12Z","article_number":"1806","intvolume":"         9","article_type":"original","volume":9,"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"quality_controlled":"1","date_created":"2023-09-06T12:07:33Z","article_processing_charge":"No","day":"04","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."}],"oa_version":"Published Version","citation":{"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>.","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.","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).","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>","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>.","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."},"pmid":1,"doi":"10.1038/s41467-018-04139-2","scopus_import":"1","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","external_id":{"pmid":["29728606"]}}