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-Structure paper
タイトル | Structures of human SGLT in the occluded state reveal conformational changes during sugar transport. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 2920, Year 2023 |
掲載日 | 2023年5月22日 |
![]() | Wenhao Cui / Yange Niu / Zejian Sun / Rui Liu / Lei Chen / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.26 - 3.48 Å |
構造データ | EMDB-33962, PDB-7yni: EMDB-33963, PDB-7ynj: EMDB-33964, PDB-7ynk: |
化合物 | ![]() ChemComp-KQC: ![]() ChemComp-GYP: |
由来 |
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![]() | PROTEIN TRANSPORT / glucose transporter / SGLT / sodium glucose transporter / membrane protein |