7N4T

Low conductance mechanosensitive channel YnaI

Summary for 7N4T

• Entry DOI: 10.2210/pdb7n4t/pdb
• EMDB information: 24177
• Descriptor: Low conductance mechanosensitive channel YnaI, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (2 entities in total)
• Functional Keywords: low conductance mechanosensitive channel ynai, ncmn, ion channel, membrane protein, transport protein
• Biological source: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
• Total number of polymer chains: 7
• Total formula weight: 276754.65

Authors

Catalano, C.,Ben-Hail, D.,Qiu, W.,des Georges, A.,Guo, Y. (deposition date: 2021-06-04, release date: 2022-04-20, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.4 Å)