7N4T

Low conductance mechanosensitive channel YnaI

7N4T の概要

• エントリーDOI: 10.2210/pdb7n4t/pdb
• EMDBエントリー: 24177
• 分子名称: Low conductance mechanosensitive channel YnaI, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (2 entities in total)
• 機能のキーワード: low conductance mechanosensitive channel ynai, ncmn, ion channel, membrane protein, transport protein
• 由来する生物種: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 276754.65

構造登録者

Catalano, C.,Ben-Hail, D.,Qiu, W.,des Georges, A.,Guo, Y. (登録日: 2021-06-04, 公開日: 2022-04-20, 最終更新日: 2024-05-29)

主引用文献

Catalano, C.,Ben-Hail, D.,Qiu, W.,Blount, P.,des Georges, A.,Guo, Y.
Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities.
Membranes (Basel), 11:-, 2021

PubMed Abstract: Mechanosensitive channels respond to mechanical forces exerted on the cell membrane and play vital roles in regulating the chemical equilibrium within cells and their environment. High-resolution structural information is required to understand the gating mechanisms of mechanosensitive channels. Protein-lipid interactions are essential for the structural and functional integrity of mechanosensitive channels, but detergents cannot maintain the crucial native lipid environment for purified mechanosensitive channels. Recently, detergent-free systems have emerged as alternatives for membrane protein structural biology. This report shows that while membrane-active polymer, SMA2000, could retain some native cell membrane lipids on the transmembrane domain of the mechanosensitive-like YnaI channel, the complete structure of the transmembrane domain of YnaI was not resolved. This reveals a significant limitation of SMA2000 or similar membrane-active copolymers. This limitation may come from the heterogeneity of the polymers and nonspecific interactions between the polymers and the relatively large hydrophobic pockets within the transmembrane domain of YnaI. However, this limitation offers development opportunities for detergent-free technology for challenging membrane proteins.

PubMed: 34832078
DOI: 10.3390/membranes11110849

実験手法

ELECTRON MICROSCOPY (2.4 Å)