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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. 2 — a cLPCAT3 cryo-EM map viewed from the lumen side of the ER membrane. The two protomers in dimeric cLPCAT3 were shown in red and blue, respectively. The non-protein electron density at the dimeric interface was shown in gray. b The cartoon representation of cLPCAT3/araCoA molecular model. The non-protein electron density in the vertical tunnel and side pocket was shown in the pink surface and the araCoA molecules that fit in the density were shown as a stick-and-ball model. Upper: the cLPCAT3 viewed parallel to the ER membrane. Lower: the cLPCAT3 viewed from the lumen side of the ER membrane. One of the promotors was colored to the same scheme as in Fig. 1c for clear observation. c The binding of the araCoA within the vertical tunnel and side pocket. The intersecting surfaces of the T-shape chamber of cLPCAT3 were shown parallel to the ER membrane at two angles. The vertical tunnel and side pocket were highlighted in green and yellow color, respectively. d The interaction of araCoA with residues in the vertical tunnel and side pocket. The catalytic residue N352 was marked with an asterisk. e The TLC assay results on the purified wild type cLPCAT3 (dark column) and araCoA-related mutants (gray columns). The enzymatic activities of mutants were normalized as the percentage of that of wild type cLPCAT3. The results were shown as mean ± s.d.; 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.