9DDN: E. coli TolAQR conformation II
E. coli TolAQR conformation II. Determined by electron microscopy at 3.18 Å resolution. Released 9 Jul 2025.
- Method
- Electron microscopy
- Resolution
- 3.18 Å
- Organism
- Escherichia coli
- Chains
- 9
- Atoms
- 9,470
- Mol. weight
- 248.04 kDa
- Released
- 9 Jul 2025
Explore 9DDN in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9DDN contains 47 α-helices and 3 β-strands across 9 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: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-12 | 3 | |
| α-helix | 15-57 | 43 | |
| α-helix | 62-70 | 9 | |
| α-helix | 73-75 | 3 | |
| α-helix | 78-95 | 18 | |
| α-helix | 101-124 | 24 | |
| α-helix | 127-154 | 28 | |
| α-helix | 164-166 | 3 | |
| α-helix | 168-220 | 53 | |
Chain B: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| α-helix | 15-57 | 43 | |
| α-helix | 62-70 | 9 | |
| α-helix | 79-94 | 16 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-156 | 30 | |
| α-helix | 164-183 | 20 | |
| α-helix | 186-221 | 36 | |
Chain C: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-12 | 6 | |
| α-helix | 15-56 | 42 | |
| α-helix | 62-70 | 9 | |
| α-helix | 78-94 | 17 | |
| α-helix | 101-116 | 16 | |
| β-strand | 117 | 1 | 1 |
| β-strand | 120 | 1 | 1 |
| β-strand | 123 | 1 | 1 |
| α-helix | 127-156 | 30 | |
| α-helix | 164-222 | 59 | |
Chain D: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-10 | 4 | |
| α-helix | 15-57 | 43 | |
| α-helix | 62-70 | 9 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-94 | 16 | |
| α-helix | 104-124 | 21 | |
| α-helix | 127-156 | 30 | |
| α-helix | 164-206 | 43 | |
| α-helix | 207-209 | 3 | |
| α-helix | 212-222 | 11 | |
Chain E: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-10 | 4 | |
| α-helix | 15-57 | 43 | |
| α-helix | 62-68 | 7 | |
| α-helix | 69-72 | 4 | |
| α-helix | 78-95 | 18 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-156 | 30 | |
| α-helix | 164-166 | 3 | |
| α-helix | 168-223 | 56 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-31 | 25 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-32 | 27 | |
Chain Y: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-35 | 17 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
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 TolA | F, G | protein | 433 | Escherichia coli | P19934 (AlphaFold model) |
| Tol-Pal system protein TolR | Y, Z | protein | 142 | Escherichia coli | P0ABV6 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>9DDN_1 Tol-Pal system protein TolQ (chains A, B, C, D, E)
MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGI
ELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNREL
ENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAI
GLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG
Sequence of entity 2 (F, G), FASTA
>9DDN_2 Tol-Pal system protein TolA (chains F, G)
MGSWSHPQFEKGSSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGGGS
SIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEK
ERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKAKAEADAKAAEEAAKKAAADAK
KKAEAEAAKAAAEAQKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAA
AEKAAADKKAAAEKAAADKKAAEKAAAEKAAADKKAAAEKAAADKKAAAAKAAAEKAAAA
KAAAEADDIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAGQIKSAI
ESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAV
YEVFKNAPLDFKP
Sequence of entity 3 (Y, Z), FASTA
>9DDN_3 Tol-Pal system protein TolR (chains Y, Z)
MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSND
NPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEI
IKALNLLHSAGVKSVGLMTQPI
Primary citation
Cryo-EM structures of the E. coli Ton and Tol motor complexes. Celia, H., Botos, I., Ghirlando, R. et al. Nat Commun (2025) 16:5506-5506. DOI 10.1038/s41467-025-61286-z · PubMed
Other PDB entries of the same protein (UniProt P0ABU9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9O40 2.92 Å, cryo-EM structure of TolQR conformation1 in SMA nanodiscs
- 9DDM 2.94 Å, E. coli TolAQR conformation I
- 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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