7AAR

sugar/H+ symporter STP10 in inward open conformation

7AAR の概要

• エントリーDOI: 10.2210/pdb7aar/pdb
• 分子名称: Sugar transport protein 10, Octyl Glucose Neopentyl Glycol, beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: membrane protein, alpha-helical protein, sugar transport, protoin/sugar symporter, major facilitator
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57595.81

構造登録者

Bavnhoej, L.,Paulsen, P.A.,Pedersen, B.P. (登録日: 2020-09-04, 公開日: 2021-08-18, 最終更新日: 2024-10-23)

主引用文献

Bavnhoj, L.,Paulsen, P.A.,Flores-Canales, J.C.,Schiott, B.,Pedersen, B.P.
Molecular mechanism of sugar transport in plants unveiled by structures of glucose/H + symporter STP10.
Nat.Plants, 7:1409-1419, 2021

PubMed Abstract: Sugars are essential sources of energy and carbon and also function as key signalling molecules in plants. Sugar transport proteins (STP) are proton-coupled symporters responsible for uptake of glucose from the apoplast into plant cells. They are integral to organ development in symplastically isolated tissues such as seed, pollen and fruit. Additionally, STPs play a vital role in plant responses to stressors such as dehydration and prevalent fungal infections like rust and mildew. Here we present a structure of Arabidopsis thaliana STP10 in the inward-open conformation at 2.6 Å resolution and a structure of the outward-occluded conformation at improved 1.8 Å resolution, both with glucose and protons bound. The two structures describe key states in the STP transport cycle. Together with molecular dynamics simulations that establish protonation states and biochemical analysis, they pinpoint structural elements, conserved in all STPs, that clarify the basis of proton-to-glucose coupling. These results advance our understanding of monosaccharide uptake, which is essential for plant organ development, and set the stage for bioengineering strategies in crops.

PubMed: 34556835
DOI: 10.1038/s41477-021-00992-0

実験手法

X-RAY DIFFRACTION (2.64 Å)