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. 2021 Jul 19;12:4376. doi: 10.1038/s41467-021-24651-2

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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 — Structures of four states are shown: “Inward-open” depicts topotecan- and 5D3-Fab- bound ABCG2 (PDB ID 7NEZ, colored in yellow), the turnover states are from this study, “ATP-bound ABCG2_E211Q” depicts the closed conformation (PDB ID: 6HBU, colored in purple). a Ribbon diagrams with substrates and ATP shown as spheres. b Surface representations of ABCG2, emphasizing the distinct TMD conformations. Red arrows depict openings to cavity 1 from within the lipid bilayer or from the cytosol. c View of substrate-binding site in cavity 1 of ABCG2. The TMDs are shown in ribbon and surface representation and viewed from the cytoplasmic side of the membrane. Substrates are shown as spheres and labeled. Red arrows depict openings to cavity 1 from within the lipid bilayer. d Surface representations of the NBDs viewed from the membrane. Bound ATP is shown as sticks. The coupling helices (CpHs) are shown as gray cartoons. Distances between CpHs are indicated.