9J2N

Cryo-EM structure of the human glucose transporter, GLUT7 in outward-facing open conformation

9J2N の概要

• エントリーDOI: 10.2210/pdb9j2n/pdb
• EMDBエントリー: 61099
• 分子名称: Solute carrier family 2, facilitated glucose transporter member 7, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: human glucose transporter 7, slc2a7, fructose transporter, intestinal hexose absorption, membrane protein, transport protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55998.40

構造登録者

Lee, S.S.,Kim, S.,Jin, M.S. (登録日: 2024-08-07, 公開日: 2024-09-25, 最終更新日: 2025-06-25)

主引用文献

Lee, S.S.,Kim, S.,Jin, M.S.
Cryo-EM structure of the human glucose transporter GLUT7.
Biochem.Biophys.Res.Commun., 738:150544-150544, 2024

PubMed Abstract: GLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human GLUT7 in the apo state at 3.3 Å resolution. Our atomic model reveals a typical major facilitator superfamily fold, with the substrate-binding site open to the extracellular side of the membrane. Despite the nearly identical conformation to its closest family member, rat GLUT5, our structure unveils distinct features of the substrate-binding cavity that may influence substrate specificity and binding mode. A homology model of the inward-open human GLUT7 indicates that similar to other members of the GLUT family, it may undergo a global rocker-switch-like reorientation of the transmembrane bundles to facilitate substrate translocation across the membrane. Our work enhances the current structural understanding of the GLUT family, and lays a foundation for rational design of regulators of GLUTs and other sugar transporters.

PubMed: 39163817
DOI: 10.1016/j.bbrc.2024.150544

実験手法

ELECTRON MICROSCOPY (3.3 Å)