9E68: MscS/YnaI chimera in DOPC nanodiscs

Cryo-EM structure of MscS/YnaI chimera in DOPC nanodiscs. Determined by electron microscopy at 2.5 Å resolution. Released 27 Aug 2025.

Method: Electron microscopy
Resolution: 2.5 Å
Organism: Escherichia coli
Chains: 7
Atoms: 10,577
Mol. weight: 241.11 kDa
Released: 27 Aug 2025

Explore 9E68 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9E68 contains 50 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.

Chain A: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	98-102	5
α-helix	105-112	8
α-helix	114-128	15
β-strand	137-138	2	2
β-strand	139	1	5
β-strand	147-152	6	2
β-strand	156-160	5	2
β-strand	166-170	5	2
α-helix	171-175	5
β-strand	179-180	2	5
α-helix	182-184	3
β-strand	188-193	6	6
β-strand	196	1	7
α-helix	201-203	3
α-helix	204-216	13
β-strand	221	1	6
β-strand	228-231	4	6
β-strand	239	1	7
β-strand	241-247	7	6
α-helix	254-272	19

Chains B, C, D, E, F and G: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	98-112	15
α-helix	114-128	15
β-strand	137-138	2	5
β-strand	139	1	8
β-strand	147-152	6	5
β-strand	156-160	5	5
β-strand	166-170	5	5
α-helix	171-175	5
β-strand	179-180	2	8
α-helix	182-184	3
β-strand	188-193	6	9
β-strand	196	1	10
α-helix	201-203	3
α-helix	204-216	13
β-strand	221	1	9
β-strand	228-231	4	9
β-strand	239	1	10
β-strand	241-247	7	9
α-helix	254-272	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MscS/YnaI chimera	A, B, C, D, E, F, G	protein	307	Escherichia coli	P0AEB5 (AlphaFold model), P0C0S1 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>9E68_1 MscS/YnaI chimera (chains A, B, C, D, E, F, G)
MEDLNVVDSINGAGSWLVANQALLLSYAVNIDFICTSLIAVILTIKLFLLINQFEKQQIK
KGRDITSARIMSRIIKITIIVVLVLLYGEHFGMSLSGLLTFGGIGGLAVGMAGKDILSNF
FSGIMLYFDRPFSIGDWIRSPDRNIEGTVAEIGWRITKITTFDNRPLYVPNSLFSSISVE
NPGRMTNRRITTTIGLRYEDAAKVGVIVEAVREMLKNHPAIDQRQTLLVYFNQFADSSLN
IMVYCFTKTTVWAEWLAAQQDVYLKIIDIVQSHGADFAFPSQTLYMDNITPPEQGRAAAL
EHHHHHH

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:

9H95 2.2 Å, YnaI in closed conformation purified in DDM with additional lipids showing ligand-filled…
9E63 2.3 Å, Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs treated with…
9E67 2.3 Å, Cryo-EM structure of mechanosensitive channel YnaI in DDPC nanodiscs
9H2P 2.3 Å, YnaI in its open conformation purified in DDM showing ligand-filled pockets
7N4T 2.4 Å, Low conductance mechanosensitive channel YnaI
9E62 2.5 Å, Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs
9H2S 2.7 Å, a YnaI-MscS chimera in a closed conformation purified in DDM with additional lipids…
9E65 2.8 Å, Cryo-EM structure of mechanosensitive channel YnaI A155V mutant in conformation 1
9E66 2.8 Å, Cryo-EM structure of mechanosensitive channel YnaI A155V mutant in conformation 2
9H2V 2.8 Å, a YnaI-MscS chimera in an open conformation purified in DDM showing ligand-filled pockets
6ZYD 3.0 Å, YnaI
9E64 3.0 Å, Cryo-EM structure of mechanosensitive channel YnaI in DOPC nanodiscs treated with…

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