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. 2019 Feb 4;9:1304. doi: 10.1038/s41598-018-37506-6

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© The Author(s) 2019

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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Molecular modeling of EfTu and SP interaction. A globular structure of B. cereus EfTu1 (UNIPROT A0A0G8DYE7), showing the typical 3 domains (I, II and III) was generated under RaptorX by alignment over Escherichia coli EfTu RCSB 1EFC (A). An unfolded structure, generated by PyMOL and submitted to CABS-flex server analysis, showed a potential rotation point between LYS296 and GLU395 (B). Both folded and unfolded models showed similar energy distribution (tension) and potential stability. The two hydrophobic barrel domains II and III of B. cereus EfTu were aligned with the trans-membrane region of OmpW and OprF using RaptorX Structure Alignment (C). Over the 165 to 193 amino acids involved in the transmembrane region of these porins, 83 were homologous in B. cereus EfTu.