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9H2P

YnaI in its open conformation purified in DDM showing ligand-filled pockets

Summary for 9H2P
Entry DOI10.2210/pdb9h2p/pdb
EMDB information51813
DescriptorLow conductance mechanosensitive channel YnaI, DODECANE (2 entities in total)
Functional Keywordsynai; mechanosensitive ion channel of e. coli; mscs-like, membrane protein
Biological sourceEscherichia coli
Total number of polymer chains7
Total formula weight269330.18
Authors
Flegler, V.J.,Bottcher, B.,Rasmussen, T.,Rasmussen, A.,Hedrich, R. (deposition date: 2024-10-14, release date: 2025-09-24)
Primary citationFlegler, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.3 Å)
Structure validation

242500

數據於2025-10-01公開中

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