9E67: Mechanosensitive channel YnaI in DDPC nanodiscs

Cryo-EM structure of mechanosensitive channel YnaI in DDPC nanodiscs. Determined by electron microscopy at 2.3 Å resolution. Released 27 Aug 2025.

Method
Electron microscopy
Resolution
2.3 Å
Organism
Escherichia coli
Chains
7
Atoms
19,033
Mol. weight
304.03 kDa
Ligands
PTY
Released
27 Aug 2025

Explore 9E67 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9E67 contains 91 α-helices and 84 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 13 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix6-116
α-helix16-3116
α-helix41-6727
α-helix75-10834
α-helix112-13423
α-helix142-15918
α-helix161-17515
β-strand184-18521
β-strand18612
β-strand194-19961
β-strand203-20751
β-strand213-21751
α-helix218-2225
β-strand226-22722
α-helix229-2313
β-strand235-24393
α-helix245-2473
α-helix251-26212
β-strand26813
β-strand275-28173
β-strand286-29493
α-helix299-31921
β-strand32413
α-helix325-3273
β-strand328-33364
Chain C: 13 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix6-116
α-helix16-3116
α-helix41-6727
α-helix75-10834
α-helix112-13322
α-helix142-15918
α-helix161-17515
β-strand184-18527
β-strand18615
β-strand194-19967
β-strand203-20757
β-strand213-21757
α-helix218-2225
β-strand226-22725
α-helix229-2313
β-strand235-24398
α-helix245-2473
α-helix251-26414
β-strand26818
β-strand275-28178
β-strand286-29498
α-helix299-31921
β-strand32418
α-helix325-3273
β-strand328-33364
Chains D, E, F and G: 13 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix6-116
α-helix16-3116
α-helix41-6727
α-helix75-10834
α-helix112-13423
α-helix142-15918
α-helix161-17515
β-strand184-18529
β-strand18617
β-strand194-19969
β-strand203-20759
β-strand213-21759
α-helix218-2225
β-strand226-22727
α-helix229-2313
β-strand235-243910
α-helix245-2473
α-helix251-26414
β-strand268110
β-strand275-281710
β-strand286-294910
α-helix299-31921
β-strand324110
α-helix325-3273
β-strand328-33364

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Low conductance mechanosensitive channel YnaIA, B, C, D, E, F, Gprotein351Escherichia coliP0AEB5 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>9E67_1 Low conductance mechanosensitive channel YnaI (chains A, B, C, D, E, F, G)
MIAELFTNNALNLVIIFGSCAALILMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSI
INYVIENYKLKFITPGVIDFICTSLIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSR
IIKITIIVVLVLLYGEHFGMSLSGLLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFS
IGDWIRSPDRNIEGTVAEIGWRITKITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTT
IGLRYEDAAKVGVIVEAVREMLKNHPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWA
EWLAAQQDVYLKIIDIVQSHGADFAFPSQTLYMDNITPPEQGRAAHHHHHH

Ligands and cofactors

IDNameFormulaCopies
PTYPhosphatidylethanolamineC40 H80 N O8 P35

Primary citation

Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI. Will, N., Hiotis, G., Nakayama, Y. et al. Nat Commun (2025) 16:7472-7472. DOI 10.1038/s41467-025-62805-8 · PubMed

Other PDB entries of the same protein (UniProt P0AEB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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