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. 2023 Sep 4;9(10):1697–1708. doi: 10.1038/s41477-023-01510-0

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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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Extended Data Fig. 9 — a, Structure alignments of ABCG25_WT and hABCG1_WT (PDB code: 7FDV), hABCG2_WT (PDB code: 6VXH) in the substrate/inhibitor-bound state. b, Superposition of the ABA-bound ABCG25, the cholesterol-bound hABCG2 (PDB code: 5NJ3) and the cholesterol-bound hABCG5/8 (PDB code: 7R8B). c, Conserved ATP-induced conformation changes between ABCG25 and ABCAs. Shown here are the representative human cholesterol transporter ABCA1 in the ATP-free (PDB code: 7TBY) and ATP-bound (PDB code: 7TBW) state, respectively. The connecting helices are indicated by the dashed-line box. The large extracellular domain of ABCA1 is hidden. The inner panel shows structure alignments of the ATP binding site in ABCG25, hABCA1 (7TBW), hABCA3(7W0W), hABCA4 (7E7Q) and ABCA7 (8EOP) in the ATP-bound state.