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. 2018 Mar 14;8:4518. doi: 10.1038/s41598-018-22842-4

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Surface potential and catalytic cleft of LC/X. (A) Left, ribbon representation of LC/X; right, surface representation of LC/X, /B, /D, /F and /Te with electrostatic potential calculated using the APBS tool in PyMol. (B) The substrate binding sites of LC/X highlighting the S an S’ sub-pockets. (C) Sequence alignment of LC/X with other VAMP-cleaving toxins. Catalytic site residues are framed in red, residues of the S an S’ sub-pockets are framed in blue and green, respectively. Stars denote amino acids involved in Zn²⁺ coordination.