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. 2017 Dec 8;7:17229. doi: 10.1038/s41598-017-17396-w

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© The Author(s) 2017

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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3D homology model of the closed EcMscL channel. (A) Single MscL subunit (rose pink) showing amino acid residues comprising the A110-S136 segment of the C-terminal bundle encompassing 27 residues subjected to cysteine scanning mutagenesis (blue spheres). The single MscL monomer is represented as a part of the channel pentamer according to the 3D homology model of EcMscL as described in the methods⁶ (left). Linear representation of the membrane topology of EcMscL (right). The N- and C-terminal domains, transmembrane helices TM1 and TM2 and the periplasmic and cytoplasmic loops are represented by rose pink and blue rectangles, respectively. (B) Sequence alignment of the C-terminal bundle of EcMscL and MtMscL. Identical residues are highlighted in black. The numerical equivalence between the residues shown in the figure was generated using a ClustalW pairwise sequence alignment between the two helical bundle sequences.