5UL7

Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant

5UL7 の概要

• エントリーDOI: 10.2210/pdb5ul7/pdb
• 関連するPDBエントリー: 5UL9 5ULD 5ULE
• 分子名称: Transporter, NadC family, SODIUM ION, SUCCINIC ACID (3 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 190806.93

構造登録者

Lu, M. (登録日: 2017-01-24, 公開日: 2017-05-17, 最終更新日: 2024-03-06)

主引用文献

Nie, R.,Stark, S.,Symersky, J.,Kaplan, R.S.,Lu, M.
Structure and function of the divalent anion/Na(+) symporter from Vibrio cholerae and a humanized variant.
Nat Commun, 8:15009-15009, 2017

PubMed Abstract: Integral membrane proteins of the divalent anion/Na symporter (DASS) family translocate dicarboxylate, tricarboxylate or sulphate across cell membranes, typically by utilizing the preexisting Na gradient. The molecular determinants for substrate recognition by DASS remain obscure, largely owing to the absence of any substrate-bound DASS structure. Here we present 2.8-Å resolution X-ray structures of VcINDY, a DASS from Vibrio cholerae that catalyses the co-transport of Na and succinate. These structures portray the Na-bound VcINDY in complexes with succinate and citrate, elucidating the binding sites for substrate and two Na ions. Furthermore, we report the structures of a humanized variant of VcINDY in complexes with succinate and citrate, which predict how a human citrate-transporting DASS may interact with its bound substrate. Our findings provide insights into metabolite transport by DASS, establishing a molecular basis for future studies on the regulation of this transport process.

PubMed: 28436435
DOI: 10.1038/ncomms15009

実験手法

X-RAY DIFFRACTION (2.8 Å)