5D0Y

Substrate bound S-component of folate ECF transporter

5D0Y の概要

• エントリーDOI: 10.2210/pdb5d0y/pdb
• 分子名称: Conserved hypothetical membrane protein, FOLIC ACID (2 entities in total)
• 機能のキーワード: ecf transporter, folate, s-component, membrane protein, vitamin, transport protein
• 由来する生物種: Lactobacillus delbrueckii subsp. bulgaricus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41921.87

構造登録者

Swier, L.J.Y.M.,Guskov, A.,Slotboom, D.J. (登録日: 2015-08-03, 公開日: 2016-04-06, 最終更新日: 2024-01-10)

主引用文献

Swier, L.J.,Guskov, A.,Slotboom, D.J.
Structural insight in the toppling mechanism of an energy-coupling factor transporter.
Nat Commun, 7:11072-11072, 2016

PubMed Abstract: Energy-coupling factor (ECF) transporters mediate uptake of micronutrients in prokaryotes. The transporters consist of an S-component that binds the transported substrate and an ECF module (EcfAA'T) that binds and hydrolyses ATP. The mechanism of transport is poorly understood but presumably involves an unusual step in which the membrane-embedded S-component topples over to carry the substrate across the membrane. In many ECF transporters, the S-component dissociates from the ECF module after transport. Subsequently, substrate-bound S-components out-compete the empty proteins for re-binding to the ECF module in a new round of transport. Here we present crystal structures of the folate-specific transporter ECF-FolT from Lactobacillus delbrueckii. Interaction of the ECF module with FolT stabilizes the toppled state, and simultaneously destroys the high-affinity folate-binding site, allowing substrate release into the cytosol. We hypothesize that differences in the kinetics of toppling can explain how substrate-loaded FolT out-competes apo-FolT for association with the ECF module.

PubMed: 27026363
DOI: 10.1038/ncomms11072

実験手法

X-RAY DIFFRACTION (3.014 Å)