9QVD: TolQRA in nanodiscs
cryo-EM structure of TolQRA in nanodiscs. Determined by electron microscopy at 3.52 Å resolution. Released 17 Dec 2025.
- Method
- Electron microscopy
- Resolution
- 3.52 Å
- Organism
- Escherichia coli str. K-12 substr. MG1655
- Chains
- 10
- Atoms
- 9,570
- Mol. weight
- 288.61 kDa
- Released
- 17 Dec 2025
Explore 9QVD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9QVD contains 48 α-helices and 0 β-strands across 10 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, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 18-56 | 39 | |
| α-helix | 62-72 | 11 | |
| α-helix | 79-96 | 18 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-158 | 32 | |
| α-helix | 168-174 | 7 | |
| α-helix | 176-219 | 44 | |
Chain B: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-11 | 6 | |
| α-helix | 15-56 | 42 | |
| α-helix | 62-72 | 11 | |
| α-helix | 79-95 | 17 | |
| α-helix | 101-123 | 23 | |
| α-helix | 128-156 | 29 | |
| α-helix | 164-218 | 55 | |
Chain C: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 15-56 | 42 | |
| α-helix | 62-69 | 8 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-96 | 18 | |
| α-helix | 101-123 | 23 | |
| α-helix | 128-158 | 31 | |
| α-helix | 168-219 | 52 | |
Chain D: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 15-56 | 42 | |
| α-helix | 62-72 | 11 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-95 | 17 | |
| α-helix | 101-123 | 23 | |
| α-helix | 128-156 | 29 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-219 | 44 | |
Chain E: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 15-56 | 42 | |
| α-helix | 62-71 | 10 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-95 | 17 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-156 | 30 | |
| α-helix | 161-162 | 2 | |
| α-helix | 164-183 | 20 | |
| α-helix | 186-219 | 34 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-34 | 14 | |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-17 | 3 | |
| α-helix | 19-34 | 16 | |
Chains H, I and J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-33 | 26 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tol-Pal system protein TolQ | A, B, C, D, E | protein | 230 | Escherichia coli str. K-12 substr. MG1655 | P0ABU9 (AlphaFold model) |
| Tol-Pal system protein TolR | F, G | protein | 142 | Escherichia coli str. K-12 substr. MG1655 | P0ABV6 (AlphaFold model) |
| Tol-Pal system protein TolA | H, I, J | protein | 421 | Escherichia coli str. K-12 substr. MG1655 | P19934 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>9QVD_1 Tol-Pal system protein TolQ (chains A, B, C, D, E)
MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGI
ELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNREL
ENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAI
GLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG
Sequence of entity 2 (F, G), FASTA
>9QVD_2 Tol-Pal system protein TolR (chains F, G)
MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSND
NPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEI
IKALNLLHSAGVKSVGLMTQPI
Sequence of entity 3 (H, I, J), FASTA
>9QVD_3 Tol-Pal system protein TolA (chains H, I, J)
MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGGGSSIDAVMVDSGAV
VEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQA
EEAAKQAELKQKQAEEAAAKAAADAKAKAEADAKAAEEAAKKAAADAKKKAEAEAAKAAA
EAQKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAA
EKAAADKKAAEKAAAEKAAADKKAAAEKAAADKKAAAAKAAAEKAAAAKAAAEADDIFGE
LSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAGQIKSAIESKFYDASSYAG
KTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFK
P
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:
- 9O40 2.92 Å, cryo-EM structure of TolQR conformation1 in SMA nanodiscs
- 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
- 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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