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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) Compact (PDB: 4XVW), (b) Transitional (PDB: 5IDR) and (c) Extended (PDB: 5ID4) crystal structures of PmScsC. Upper panels: side view, secondary structure with catalytic domains in green, 11-residue peptide linker in cyan and trimerization domains in magenta or white. Height in this orientation is indicated. In each case, one trimerization domain is shown in magenta for comparison of the conformational changes across the three crystal structures. Lower panels: top view, surface representation (catalytic TRX fold domains green, trimerization domains white), maximum dimension in this orientation is labelled. Active site positions are indicated in orange for each protomer.