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. 2017 Jul 19;8:16065. doi: 10.1038/ncomms16065

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Copyright © 2017, The Author(s)

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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(a) Linear representation of the domain organization of PmScsC mutants. The trimerization domain is coloured magenta, the catalytic domain is green, with the CXXC motif represented as an orange circle, and the linker region is shown in cyan. The rigid helical linker is shown in black. (b) Swarming motility of wild type P. mirabilis strain PM54 (black), PmScsC deletion mutant PM54scsC (grey) and PM54scsC containing control and complementation plasmids: PM54scsC(pSU2718) (vector control; cyan), PM54scsC(pScsC) (wild-type; green), PM54scsC (pScsC AXXC) (active site mutant; orange) and PM54scsC(pScsCΔN) (N-terminal trimerization domain deletion; magenta) in the presence of 1.5 mM CuSO₄ on LB agar plates (significant difference, P<0.0001 for slope calculated by F-test). Data are shown as the mean±s.d., of a single experiment performed in triplicate; all data is representative of three independent experiments. (c) Disulfide isomerase activity of PmScsC (hollow squares) is similar to that of EcDsbC (filled circles). Monomeric PmScsΔN (filled squares) and the PmScsC mutant engineered to have a rigid helical peptide (RHP) in place of the flexible peptide (filled diamonds) show negligible activity (equivalent to oxidase EcDsbA (hollow circles)). Data are shown as the mean±s.d., of two replicate experiments.