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. 2018 Feb 15;9:231. doi: 10.3389/fmicb.2018.00231

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Copyright © 2018 Su, Su, Liu, Zhang, He, Huang, Xu and Gu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Overall structure of BdsA. (A) The four BdsA monomers (A, B, C, and D) forming two homodimers are designated with cartoon in different colors. (B) The secondary structures (13 α-helices and 9 β-strands) of BdsA monomer are depicted in rainbow colored cartoon. (C) Structure of BdsA dimer. The dimer is shown in cartoon model. Molecule A is in gray color and molecule B is in blue color. The dimer interface consists of α1, IS1, IS2, α2, α3, IS3, and IS4. IS5 separated from the protein core is located between α7 and β8, which contains four small helices (α8, α9, α10, and α11).