6WTW

Structure of LaINDY crystallized in the presence of alpha-ketoglutarate and malate

6WTW の概要

• エントリーDOI: 10.2210/pdb6wtw/pdb
• 分子名称: DASS family sodium-coupled anion symporter (1 entity in total)
• 機能のキーワード: transporter, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, membrane protein, transport protein
• 由来する生物種: Lactobacillus acidophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107079.05

構造登録者

Sauer, D.B.,Cocco, N.,Marden, J.J.,Song, J.M.,Wang, D.N.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2020-05-04, 公開日: 2020-09-16, 最終更新日: 2023-10-18)

主引用文献

Sauer, D.B.,Trebesch, N.,Marden, J.J.,Cocco, N.,Song, J.,Koide, A.,Koide, S.,Tajkhorshid, E.,Wang, D.N.
Structural basis for the reaction cycle of DASS dicarboxylate transporters.
Elife, 9:-, 2020

PubMed Abstract: Citrate, α-ketoglutarate and succinate are TCA cycle intermediates that also play essential roles in metabolic signaling and cellular regulation. These di- and tricarboxylates are imported into the cell by the divalent anion sodium symporter (DASS) family of plasma membrane transporters, which contains both cotransporters and exchangers. While DASS proteins transport substrates via an elevator mechanism, to date structures are only available for a single DASS cotransporter protein in a substrate-bound, inward-facing state. We report multiple cryo-EM and X-ray structures in four different states, including three hitherto unseen states, along with molecular dynamics simulations, of both a cotransporter and an exchanger. Comparison of these outward- and inward-facing structures reveal how the transport domain translates and rotates within the framework of the scaffold domain through the transport cycle. Additionally, we propose that DASS transporters ensure substrate coupling by a charge-compensation mechanism, and by structural changes upon substrate release.

PubMed: 32869741
DOI: 10.7554/eLife.61350

実験手法

X-RAY DIFFRACTION (2.86 Å)