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. 2018 Jan 18;8:1103. doi: 10.1038/s41598-018-19429-4

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© The Author(s) 2018

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) Schematic drawing of the domain arrangement of PDIA1 and PDIA3 in which the CGHC-motive of the catalytically active sites are indicated. (B) Schematic domain arrangement of the 2 TRAP mutant of PDIA6, where both C-terminal cysteine residues of the CGHC-motive are exchanged to serine residues. (C) Schematic drawing of the C55SC58S mutant and (D) the inverse TRAP mutant bearing exchanges in the N-terminal cysteine residues of the CGHC-motive. (E) Chromatograms of the SEC-MALS analysis of PDIA1, PDIA3, PDIA6 and BSA as control. Shown is only the relevant section of the complete elution profile (60 minutes at 0.5 ml/minutes) of the detected absorption at 280 nm (dashed line) and the Rayleigh ratio (solid line, derived from MALS) normalized to PDIA6. In addition, the calculated molecular weight for each slice of the analyzed peaks is shown. (F) Comparison of the activities of indicated TRAP mutants relative to wild-type PDIA6 whose activity was set to 100%.