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. 2015 Aug 14;15:163. doi: 10.1186/s12866-015-0498-1

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© Bulir et al. 2015

Open Access This 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. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 3 — LcrH_1 (Cpn0811) interacts with CopB. (a) Recombinant LcrH_1 interacted with amino acids 1–200 of CopB. CopB mutants were created using Gblock synthesis: ^P166ACopB_1–200, ^L168ACopB_1–200, and ^P171ACopD_1–200. (b & c) Mutations at the conserved amino acids within the predicted chaperone binding domain disrupted the interaction between CopB_1–200 and the chaperone LcrH_1, but not other identified interactions