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. 2021 Nov 25;12:6869. doi: 10.1038/s41467-021-27244-1

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© The Author(s) 2021

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 — a The cartoon representation of the cLPCAT3/LPC molecular model as viewed parallel to the ER membrane. The non-protein electron density in the horizontal tunnel was shown in the green surface and the LPC (12:0) molecules that fit in the density were shown as a stick-and-ball model. b The binding of the LPC molecule within the horizontal tunnel. The intersecting surfaces of the T-shape chamber of cLPCAT3 were shown parallel to the ER membrane. The horizontal tunnel was highlighted in pink. c The interaction of LPC with residues in the horizontal tunnel. The catalytic residue H388 was marked with an asterisk. d The TLC assay results on the purified wild type cLPCAT3 (dark column) and LPP-related mutants (gray columns). The enzymatic activities of mutants were normalized as the percentage of that of the wild type cLPCAT3. The results were shown as mean ± s.d. of experiments, n = 3 independent experiments for all mutants. One-way ANOVA with Dunnett’s multiple comparisons test was applied and the 95% CI was calculated by Graphpad Prism (version 6.01) and p-values were labeled above the histogram.