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. 2023 Oct 16;8(11):2050–2066. doi: 10.1038/s41564-023-01498-5

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© The Author(s) 2023

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. 1 — a, Secondary structure prediction of FcR1 with key residues highlighted: proton acceptor D-121 and donor E-132 (black), K-261 (pink) forming a Schiff base link with retinal, and retinal binding pocket (Y-119, W-122, V-126, L-129, A-160, I-161, G-165, W-181, A-184, M-185, F-188, W-226, Y-229, P-230, Y-233, Y-253 and S-260) (light grey). The N-terminal extension of 30 amino acids of FcR1 compared to FcR2 is indicated as a dotted line. Potential N-terminal chloroplast signal peptide with conserved ‘ASAFAP’ (red circles) and lysine-rich motif (orange diamonds) in the N terminus of FcR1 are highlighted. Grey boxes correspond to transmembrane helices as predicted by AlphaFold2 structure prediction in b. b, Overall 3D view of the FcR1 protomer in the membrane as predicted by AlphaFold2. The experimental structure of PDB entry 4HYJ⁴² was used for structural alignment with FcR1 to position the retinal ligand, and the final model was generated by removing the structure of PDB entry 4HYJ. Estimated hydrophobic–hydrophilic membrane boundaries are shown as light blue lines.

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