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8BB6

Crystal structure of Arabidopsis thaliana sucrose transporter SUC1

8BB6 の概要
エントリーDOI10.2210/pdb8bb6/pdb
分子名称Sucrose transport protein SUC1 (2 entities in total)
機能のキーワードplant sucrose/proton symporter, major facilitator superfamily, membrane protein
由来する生物種Arabidopsis thaliana (thale cress)
タンパク質・核酸の鎖数2
化学式量合計110971.35
構造登録者
Bavnhoej, L.,Pedersen, B.P. (登録日: 2022-10-12, 公開日: 2023-05-31, 最終更新日: 2024-11-06)
主引用文献Bavnhoj, L.,Driller, J.H.,Zuzic, L.,Stange, A.D.,Schiott, B.,Pedersen, B.P.
Structure and sucrose binding mechanism of the plant SUC1 sucrose transporter.
Nat.Plants, 9:938-950, 2023
Cited by
PubMed Abstract: Sucrose import from photosynthetic tissues into the phloem is mediated by transporters from the low-affinity sucrose transporter family (SUC/SUT family). Furthermore, sucrose redistribution to other tissues is driven by phloem sap movement, the product of high turgor pressure created by this import activity. Additionally, sink organs such as fruits, cereals and seeds that accumulate high concentrations of sugar also depend on this active transport of sucrose. Here we present the structure of the sucrose-proton symporter, Arabidopsis thaliana SUC1, in an outward open conformation at 2.7 Å resolution, together with molecular dynamics simulations and biochemical characterization. We identify the key acidic residue required for proton-driven sucrose uptake and describe how protonation and sucrose binding are strongly coupled. Sucrose binding is a two-step process, with initial recognition mediated by the glucosyl moiety binding directly to the key acidic residue in a stringent pH-dependent manner. Our results explain how low-affinity sucrose transport is achieved in plants, and pinpoint a range of SUC binders that help define selectivity. Our data demonstrate a new mode for proton-driven symport with links to cation-driven symport and provide a broad model for general low-affinity transport in highly enriched substrate environments.
PubMed: 37188854
DOI: 10.1038/s41477-023-01421-0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.68 Å)
構造検証レポート
Validation report summary of 8bb6
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-04に公開中

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