6LEP

Crystal structure of thiosulfate transporter YeeE inactive mutant - C91A

6LEP の概要

• エントリーDOI: 10.2210/pdb6lep/pdb
• 分子名称: Sulf_transp domain-containing protein, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, THIOSULFATE, ... (4 entities in total)
• 機能のキーワード: transmembrane, transporter, transport protein
• 由来する生物種: Spirochaeta thermophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37907.94

構造登録者

Tanaka, Y.,Tsukazaki, T.,Yoshikaie, K.,Sugano, Y.,Takeuchi, A.,Uchino, S. (登録日: 2019-11-26, 公開日: 2020-09-02, 最終更新日: 2024-04-03)

主引用文献

Tanaka, Y.,Yoshikaie, K.,Takeuchi, A.,Ichikawa, M.,Mori, T.,Uchino, S.,Sugano, Y.,Hakoshima, T.,Takagi, H.,Nonaka, G.,Tsukazaki, T.
Crystal structure of a YeeE/YedE family protein engaged in thiosulfate uptake.
Sci Adv, 6:eaba7637-eaba7637, 2020

PubMed Abstract: We have demonstrated that a bacterial membrane protein, YeeE, mediates thiosulfate uptake. Thiosulfate is used for cysteine synthesis in bacteria as an inorganic sulfur source in the global biological sulfur cycle. The crystal structure of YeeE at 2.5-Å resolution reveals an unprecedented hourglass-like architecture with thiosulfate in the positively charged outer concave side. YeeE is composed of loops and 13 helices including 9 transmembrane α helices, most of which show an intramolecular pseudo 222 symmetry. Four characteristic loops are buried toward the center of YeeE and form its central region surrounded by the nine helices. Additional electron density maps and successive molecular dynamics simulations imply that thiosulfate can remain temporally at several positions in the proposed pathway. We propose a plausible mechanism of thiosulfate uptake via three important conserved cysteine residues of the loops along the pathway.

PubMed: 32923628
DOI: 10.1126/sciadv.aba7637

実験手法

X-RAY DIFFRACTION (2.6 Å)