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PA must be cleaved by host proteases before it oligomerizes and forms a prepore, to which LF and EF bind. After endocytosis of this tripartite complex, the prepore transforms into a narrow transmembrane pore that delivers unfolded LF and EF into the host cytosol. Here, we find that translocation of multiple 90-kD LF molecules is rapid and efficient. To probe the molecular basis of this translocation, we calculated a three-dimensional map of the fully loaded (PA63)7\u2013(LF)3 prepore complex by cryo\u2013electron microscopy (cryo-EM). The map shows three LFs bound in a similar way to one another, via their N-terminal domains, to the surface of the PA heptamer. The model also reveals contacts between the N- and C-terminal domains of adjacent LF molecules. We propose that this molecular arrangement plays an important role in the maintenance of translocation efficiency through the narrow PA pore.<\/jats:p>","DOI":"10.1085\/jgp.201611617","type":"journal-article","created":{"date-parts":[[2016,9,26]],"date-time":"2016-09-26T13:39:43Z","timestamp":1474897183000},"page":"313-324","update-policy":"https:\/\/doi.org\/10.1085\/jgp.crossmarkpolicy","source":"Crossref","is-referenced-by-count":17,"title":["Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry"],"prefix":"10.1085","volume":"148","author":[{"given":"Lucien","family":"Fabre","sequence":"first","affiliation":[{"name":"Department of Anatomy and Cell Biology, McGill University, Montr\u00e9al, Qu\u00e9bec H3A 0C7, Canada 1"},{"name":"Groupe de Recherche Ax\u00e9 sur la Structure des Prot\u00e9ines (GRASP), Groupe d\u2019\u00c9tude des Prot\u00e9ines Membranaires (G\u00c9PROM), McGill University, Montr\u00e9al, Qu\u00e9bec H3A 0C7, Canada 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