9H2S

a YnaI-MscS chimera in a closed conformation purified in DDM with additional lipids showing ligand-filled pore and pockets

9H2S の概要

• エントリーDOI: 10.2210/pdb9h2s/pdb
• EMDBエントリー: 51817
• 分子名称: Low conductance mechanosensitive channel YnaI,Small-conductance mechanosensitive channel, DODECANE (2 entities in total)
• 機能のキーワード: chimera; mechanosensitive ion channel; mscs-like, membrane protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 258718.56

構造登録者

Flegler, V.J.,Bottcher, B.,Rasmussen, T.,Rasmussen, A.,Hedrich, R. (登録日: 2024-10-15, 公開日: 2025-09-24)

主引用文献

Flegler, V.J.,Rasmussen, A.,Hedrich, R.,Rasmussen, T.,Bottcher, B.
Mechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.
Nat Commun, 16:7881-7881, 2025

PubMed Abstract: Osmotically varying environments are challenging for bacterial cells. Sudden drops in osmolytes cause an increased membrane tension and rupture the cells in the absence of protective mechanisms. One family of protective proteins are mechanosensitive channels of small conductance that open in response to membrane tension. Although these channels have a common architecture, they vary widely in the number of transmembrane helices, conductivity, and gating characteristics. Although there are various structures of channels in the open and closed state, the underlying common principles of the gating mechanism remain poorly understood. Here we show that YnaI opens by radial relocation of the transmembrane sensor paddles together with a shortening of the pore, which contrasts the prototypic smaller MscS. A chimera of both channels with the YnaI sensor paddles and the pore containing C-terminal part of MscS is functional and has the tension response of the paddle donor. Our research shows that elements with different structural opening mechanisms can be mixed and matched within one channel as long as they support the common area expansion on the periplasmic side.

PubMed: 40849500
DOI: 10.1038/s41467-025-63253-0

実験手法

ELECTRON MICROSCOPY (2.7 Å)