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. 2010 Jun 14;2(6):1445–1470. doi: 10.3390/toxins2061445

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© 2010 by the authors; licensee MDPI, Basel, Switzerland

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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The structure and subunit organization of LT. (A) The crystal structure of LT holotoxin, generated using Swiss-PDB viewer (version 4.0.1) using PDB number 1LTA. The globular A1 fragment and the helical A2 peptide can be seen in blue, along with a ring of five B subunits. (B) A schematic of the subunit organization of LT. (C) A schematic of LT showing a cutaway view of the toxin’s central core. The location of the site of proteolytic processing (“nicking”), which is subtended by a disulfide bond, is circled. Nicking occurs after secretion of the toxin, and the disulfide is reduced inside the host cell, releasing the catalytically active A1 fragment.