6H7D

Crystal Structure of A. thaliana Sugar Transport Protein 10 in complex with glucose in the outward occluded state

6H7D の概要

• エントリーDOI: 10.2210/pdb6h7d/pdb
• 分子名称: Sugar transport protein 10, beta-D-glucopyranose, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, ... (6 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 (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59320.85

構造登録者

Pedersen, B.P.,Paulsen, P.A.,Custodio, T.F. (登録日: 2018-07-31, 公開日: 2019-02-06, 最終更新日: 2024-10-09)

主引用文献

Paulsen, P.A.,Custodio, T.F.,Pedersen, B.P.
Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily.
Nat Commun, 10:407-407, 2019

PubMed Abstract: Plants are dependent on controlled sugar uptake for correct organ development and sugar storage, and apoplastic sugar depletion is a defense strategy against microbial infections like rust and mildew. Uptake of glucose and other monosaccharides is mediated by Sugar Transport Proteins, proton-coupled symporters from the Monosaccharide Transporter (MST) superfamily. We present the 2.4 Å structure of Arabidopsis thaliana high affinity sugar transport protein, STP10, with glucose bound. The structure explains high affinity sugar recognition and suggests a proton donor/acceptor pair that links sugar transport to proton translocation. It contains a Lid domain, conserved in all STPs, that locks the mobile transmembrane domains through a disulfide bridge, and creates a protected environment which allows efficient coupling of the proton gradient to drive sugar uptake. The STP10 structure illuminates fundamental principles of sugar transport in the MST superfamily with implications for both plant antimicrobial defense, organ development and sugar storage.

PubMed: 30679446
DOI: 10.1038/s41467-018-08176-9

実験手法

X-RAY DIFFRACTION (2.4 Å)