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. 2017 Nov 16;8:1529. doi: 10.1038/s41467-017-01671-5

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© The Author(s) 2017

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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Fig. 3 — Effects of FolD mutations on DH activity and carolacton binding. a Residual DH activity of ecFolD mutants compared to ecFolD. Data are presented as means ± s.e.m of three independent replicates. DH specific activities were calculated based on the V _max obtained via Michaelis–Menten fitting. The one-way ANOVA test was used for statistical analysis, P < 0.01. b IC₅₀ determination for carolacton against the DH activity of ecFolD and mutants. Data are presented as means ± s.e.m of three independent replicates. IC₅₀s were obtained via logistic dose–response fitting. The one-way ANOVA test was used for statistical analysis, P < 0.01. c Position of Y50 in ecFolDQ98H (gold). The position of Q98 in the apo (grey) and complex (blue) structures prevents the side-chain of Y50 from rotating out of position. d Position of Y50 in the apo (grey), complex (blue) and Q98H (gold) structures. The 90° rotation of Y50 in the Q98H mutant prevents Y50 from forming the hydrophobic lid on carolacton (lime sticks)