7YNJ

Structure of human SGLT2-MAP17 complex bound with substrate AMG in the occluded conformation

7YNJ の概要

• エントリーDOI: 10.2210/pdb7ynj/pdb
• EMDBエントリー: 33963
• 分子名称: Sodium/glucose cotransporter 2, PDZK1-interacting protein 1, methyl alpha-D-glucopyranoside (3 entities in total)
• 機能のキーワード: glucose transporter, sglt, sodium glucose transporter, membrane protein, protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85378.60

構造登録者

Chen, L.,Niu, Y.,Cui, W. (登録日: 2022-07-31, 公開日: 2023-05-31, 最終更新日: 2025-06-25)

主引用文献

Cui, W.,Niu, Y.,Sun, Z.,Liu, R.,Chen, L.
Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.
Nat Commun, 14:2920-2920, 2023

PubMed Abstract: Sodium-Glucose Cotransporters (SGLT) mediate the uphill uptake of extracellular sugars and play fundamental roles in sugar metabolism. Although their structures in inward-open and outward-open conformations are emerging from structural studies, the trajectory of how SGLTs transit from the outward-facing to the inward-facing conformation remains unknown. Here, we present the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound state. Both structures show an occluded conformation, with not only the extracellular gate but also the intracellular gate tightly sealed. The sugar substrate are caged inside a cavity surrounded by TM1, TM2, TM3, TM6, TM7, and TM10. Further structural analysis reveals the conformational changes associated with the binding and release of substrates. These structures fill a gap in our understanding of the structural mechanisms of SGLT transporters.

PubMed: 37217492
DOI: 10.1038/s41467-023-38720-1

実験手法

ELECTRON MICROSCOPY (3.33 Å)