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. 2017 May 11;8(8):623–627. doi: 10.1007/s13238-017-0417-3

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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.

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AcrB structure and mutation sites. (A) Trimer crystal structure of E. coli AcrB (PDB ID: 4DX5). One protomer is shown in color, and the other two in grey. The N_TM and C_TM subdomains are shown in wheat color and cyan, respectively. The porter domain and docking domain are in yellow. The cytosolic-side amphipathic helix, α6-7, is colored in orange. (B) The signaling motif-C in C_TM. The three main-chain H-bonds are depicted as dash-lines. Except proline residues, side-chains are omitted for clarity. (C) The α6-7 region. (D) Region of the titratable key residue(s)