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. 2022 May 12;13:2632. doi: 10.1038/s41467-022-30326-3

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© The Author(s) 2022

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. 5 — a Structural comparison of GLUT3 bound to SA47 and maltose. Left: The NTD and CTD of GLUT3-SA47 were colored yellow and cyan, respectively. GLUT3-maltose structure (PDB code: 4ZWC) was colored gray. Despite the much larger size of SA47 than maltose, the overall structure of GLUT3 remains nearly unchanged in the presence of these two inhibitors. The SA47 was shown as ball-and-sticks and colored gray. The maltose was shown as stick and colored green. Glc1: the first glucose unit; Glc2: the second glucose unit. Right: Residue shifts of TM7b upon SA47 binding. Phe289 and Asn286 on TM7b undergo minor shifts between the two structures. Shown here is an extracellular view of the superimposed structures of GLUT3 bound to SA47 (domain colored) and maltose (gray, PDB code: 4ZWC). The glc2 moiety of maltose is highlighted by colored orange. b Structural comparison of the outward-facing GLUT3-SA47 and inward-facing GLUT1-CCB. SA47 and CCB were positioned based on overall structural superposition of GLUT1-CCB (PDB code: 5EQI) and GLUT3-SA47.