{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T07:36:32Z","timestamp":1791012992362,"version":"4.1.0"},"reference-count":41,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2011,3,28]],"date-time":"2011-03-28T00:00:00Z","timestamp":1301270400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2011,5]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The essential cellular functions of secretion and protein degradation require a molecular machine to unfold and translocate proteins either across a membrane or into a proteolytic complex. Protein translocation is also critical for microbial pathogenesis, namely bacteria can use translocase channels to deliver toxic proteins into a target cell. Anthrax toxin (Atx), a key virulence factor secreted by <jats:italic>Bacillus anthracis<\/jats:italic>, provides a robust biophysical model to characterize transmembrane protein translocation. Atx is comprised of three proteins: the translocase component, protective antigen (PA) and two enzyme components, lethal factor (LF) and oedema factor (OF). Atx forms an active holotoxin complex containing a ring\u2010shaped PA oligomer bound to multiple copies of LF and OF. These complexes are endocytosed into mammalian host cells, where PA forms a protein\u2010conducting translocase channel. The proton motive force unfolds and translocates LF and OF through the channel. Recent structure and function studies have shown that LF unfolds during translocation in a force\u2010dependent manner via a series of metastable intermediates. Polypeptide\u2010binding clamps located throughout the PA channel catalyse substrate unfolding and translocation by stabilizing unfolding intermediates through the formation of a series of interactions with various chemical groups and \u03b1\u2010helical structure presented by the unfolding polypeptide during translocation.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07614.x","type":"journal-article","created":{"date-parts":[[2011,3,28]],"date-time":"2011-03-28T15:15:12Z","timestamp":1301325312000},"page":"588-595","source":"Crossref","is-referenced-by-count":66,"title":["The unfolding story of anthrax toxin translocation"],"prefix":"10.1111","volume":"80","author":[{"given":"Katie L.","family":"Thoren","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bryan 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