9O40: TolQR conformation1 in SMA nanodiscs

cryo-EM structure of TolQR conformation1 in SMA nanodiscs. Determined by electron microscopy at 2.92 Å resolution. Released 17 Dec 2025.

Method: Electron microscopy
Resolution: 2.92 Å
Organism: Escherichia coli
Chains: 7
Atoms: 8,967
Mol. weight: 158.92 kDa
Released: 17 Dec 2025

Explore 9O40 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O40 contains 41 α-helices and 0 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: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	6-12	7
α-helix	15-58	44
α-helix	62-70	9
α-helix	79-96	18
α-helix	103-123	21
α-helix	128-156	29
α-helix	168-221	54

Chain B: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	6-12	7
α-helix	15-56	42
α-helix	62-71	10
α-helix	79-96	18
α-helix	103-122	20
α-helix	127-158	32
α-helix	164-221	58

Chain C: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	6-11	6
α-helix	15-58	44
α-helix	62-71	10
α-helix	79-94	16
α-helix	101-123	23
α-helix	128-158	31
α-helix	164-221	58

Chain D: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	6-11	6
α-helix	15-57	43
α-helix	62-71	10
α-helix	79-96	18
α-helix	101-122	22
α-helix	127-158	32
α-helix	168-173	6
α-helix	176-221	46

Chain E: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	6-12	7
α-helix	15-57	43
α-helix	62-69	8
α-helix	70-72	3
α-helix	79-96	18
α-helix	103-123	21
α-helix	127-136	10
α-helix	138-158	21
α-helix	164-166	3
α-helix	168-221	54

Chains F and G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	19-35	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tol-Pal system protein TolQ	A, B, C, D, E	protein	230	Escherichia coli	P0ABU9 (AlphaFold model)
Tol-Pal system protein TolR	F, G	protein	142	Escherichia coli	P0ABV6 (AlphaFold model)

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

>9O40_1 Tol-Pal system protein TolQ (chains A, B, C, D, E)
MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGI
ELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNREL
ENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAI
GLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG

Sequence of entity 2 (F, G), FASTA

>9O40_2 Tol-Pal system protein TolR (chains F, G)
MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSND
NPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEI
IKALNLLHSAGVKSVGLMTQPI

Primary citation

Deciphering the molecular mechanism of the bacterial division motor TolQRA. Shen, C., Xie, T., Luo, Y. et al. Cell Discov (2025) 11:87-87. DOI 10.1038/s41421-025-00841-w · PubMed

Other PDB entries of the same protein (UniProt P0ABU9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9DDM 2.94 Å, E. coli TolAQR conformation I
9DDN 3.18 Å, E. coli TolAQR conformation II
9KPZ 3.18 Å, Structure of TolQRA complex at pH 5.4 from E.coli
9QUQ 3.28 Å, cryo-EM structure of TolQR conformation2 in SMA nanodiscs
9QVD 3.52 Å, cryo-EM structure of TolQRA in nanodiscs
9K49 3.6 Å, Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent…
9KQ0 3.6 Å, Structure of TolQRA complex at pH 8.0 from E.coli
9KCH 4.19 Å, Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent…
8ODT 4.2 Å, Structure of TolQR complex from E.coli

Browse structure collections

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