5A1S

Crystal structure of the sodium-dependent citrate symporter SeCitS form Salmonella enterica.

5A1S の概要

• エントリーDOI: 10.2210/pdb5a1s/pdb
• 分子名称: CITRATE-SODIUM SYMPORTER, SODIUM ION, CITRATE ANION, ... (9 entities in total)
• 機能のキーワード: transport protein, membrane protein, symporter, transporter, di-carboxylate transporter
• 由来する生物種: SALMONELLA ENTERICA
• 細胞内の位置: Cell membrane : G4BX92
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 195945.57

構造登録者

Woehlert, D.,Groetzinger, M.J.,Kuhlbrandt, W.,Yildiz, O. (登録日: 2015-05-05, 公開日: 2016-02-17, 最終更新日: 2024-05-08)

主引用文献

Wohlert, D.,Grotzinger, M.J.,Kuhlbrandt, W.,Yildiz, O.
Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer.
Elife, 4:e09375-e09375, 2015

PubMed Abstract: The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 Å x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-facing states. All three states resolve the substrates in their respective binding environments. Together with comprehensive functional studies on reconstituted proteoliposomes, the structures explain the transport mechanism in detail. Our results indicate a six-step process, with a rigid-body 31° rotation of a helix bundle that translocates the bound substrates by 16 Å across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets.

PubMed: 26636752
DOI: 10.7554/eLife.09375

実験手法

X-RAY DIFFRACTION (2.5 Å)