6E9N

E. coli D-galactonate:proton symporter in the inward open form

6E9N の概要

• エントリーDOI: 10.2210/pdb6e9n/pdb
• 分子名称: D-galactonate transport, D-gluconic acid, nonyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: mfs transporter, slc17, organic anion transporter, membrane protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102734.85

構造登録者

Leano, J.B.,Edwards, R.H.,Stroud, R.M. (登録日: 2018-08-01, 公開日: 2019-05-22, 最終更新日: 2023-10-11)

主引用文献

Leano, J.B.,Batarni, S.,Eriksen, J.,Juge, N.,Pak, J.E.,Kimura-Someya, T.,Robles-Colmenares, Y.,Moriyama, Y.,Stroud, R.M.,Edwards, R.H.
Structures suggest a mechanism for energy coupling by a family of organic anion transporters.
Plos Biol., 17:e3000260-e3000260, 2019

PubMed Abstract: Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane.

PubMed: 31083648
DOI: 10.1371/journal.pbio.3000260

実験手法

X-RAY DIFFRACTION (2.915 Å)