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9E63

Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs treated with beta-cyclodextrin

Summary for 9E63
Entry DOI10.2210/pdb9e63/pdb
Related9E62
EMDB information47547 47548
DescriptorLow conductance mechanosensitive channel YnaI, PHOSPHATIDYLETHANOLAMINE (2 entities in total)
Functional Keywordsmechanosensitive, membrane protein
Biological sourceEscherichia coli
Total number of polymer chains7
Total formula weight304034.96
Authors
Hiotis, G.,Will, N.,Walz, T. (deposition date: 2024-10-29, release date: 2025-08-27)
Primary citationWill, N.,Hiotis, G.,Nakayama, Y.,Angiulli, G.,Zhou, Z.,Cox, C.D.,Martinac, B.,Walz, T.
Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI.
Nat Commun, 16:7472-7472, 2025
Cited by
PubMed Abstract: YnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been extensively studied for MscS, but are less well understood for YnaI, which features two additional transmembrane helices. Here, we combined cryogenic electron microscopy, molecular dynamics simulations and patch-clamp electrophysiology to advance our understanding of YnaI. The two additional helices move the lipid-filled hydrophobic pockets in YnaI further away from the lipid bilayer and change the function of the pocket lipids from being a critical gating element in MscS to being more of a structural element in YnaI. Unlike MscS, YnaI shows pronounced gating hysteresis and remains open to a substantially lower membrane tension than is needed to initially open the channel. Thus, at near-lytic membrane tension, both MscL and YnaI will open, but while MscL has a large pore and must close quickly to minimize loss of essential metabolites, YnaI only conducts ions and can thus remain open for longer to continue to facilitate pressure equilibration across the membrane.
PubMed: 40796571
DOI: 10.1038/s41467-025-62805-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.3 Å)
Structure validation

240971

數據於2025-08-27公開中

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