9KCH: Tol-Pal system protein TolQ
Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles. Determined by electron microscopy at 4.19 Å resolution. Released 9 Jul 2025.
- Method
- Electron microscopy
- Resolution
- 4.19 Å
- Organism
- Escherichia coli K-12
- Chains
- 8
- Atoms
- 9,121
- Mol. weight
- 204.84 kDa
- Released
- 9 Jul 2025
Explore 9KCH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9KCH contains 44 α-helices and 0 β-strands across 8 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: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-56 | 40 | |
| α-helix | 62-68 | 7 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-96 | 18 | |
| α-helix | 104-123 | 20 | |
| α-helix | 127-134 | 8 | |
| α-helix | 137-155 | 19 | |
| α-helix | 160-162 | 3 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-181 | 14 | |
| α-helix | 185-221 | 37 | |
Chain B: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-55 | 41 | |
| α-helix | 62-71 | 10 | |
| α-helix | 80-95 | 16 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-158 | 32 | |
| α-helix | 168-219 | 52 | |
Chain C: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-56 | 42 | |
| α-helix | 62-70 | 9 | |
| α-helix | 79-94 | 16 | |
| α-helix | 104-123 | 20 | |
| α-helix | 127-158 | 32 | |
| α-helix | 168-223 | 56 | |
Chain D: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-56 | 42 | |
| α-helix | 62-69 | 8 | |
| α-helix | 70-72 | 3 | |
| α-helix | 78-95 | 18 | |
| α-helix | 101-123 | 23 | |
| α-helix | 127-156 | 30 | |
| α-helix | 168-183 | 16 | |
| α-helix | 185-221 | 37 | |
Chain E: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-56 | 35 | |
| α-helix | 62-70 | 9 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-95 | 17 | |
| α-helix | 101-103 | 3 | |
| α-helix | 104-124 | 21 | |
| α-helix | 127-143 | 17 | |
| α-helix | 145-154 | 10 | |
| α-helix | 168-183 | 16 | |
| α-helix | 185-221 | 37 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-30 | 10 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-33 | 15 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-32 | 24 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tol-Pal system protein TolQ | A, B, C, D, E | protein | 230 | Escherichia coli K-12 | P0ABU9 (AlphaFold model) |
| Tol-Pal system protein TolR | F, G | protein | 152 | Escherichia coli K-12 | P0ABV6 (AlphaFold model) |
| Tol-Pal system protein TolA | H | protein | 421 | Escherichia coli K-12 | P19934 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>9KCH_1 Tol-Pal system protein TolQ (chains A, B, C, D, E)
MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGI
ELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNREL
ENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAI
GLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG
Sequence of entity 2 (F, G), FASTA
>9KCH_2 Tol-Pal system protein TolR (chains F, G)
MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSND
NPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEI
IKALNLLHSAGVKSVGLMTQPILEHHHHHHHH
Sequence of entity 3 (H), FASTA
>9KCH_3 Tol-Pal system protein TolA (chains H)
MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGGGSSIDAVMVDSGAV
VEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQA
EEAAKQAELKQKQAEEAAAKAAADAKAKAEADAKAAEEAAKKAAADAKKKAEAEAAKAAA
EAQKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAA
EKAAADKKAAEKAAAEKAAADKKAAAEKAAADKKAAAAKAAAEKAAAAKAAAEADDIFGE
LSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAGQIKSAIESKFYDASSYAG
KTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFK
P
Primary citation
Structural Insights into the Force-Transducing Mechanism of a Motor-Stator Complex Important for Bacterial Outer Membrane Lipid Homeostasis. Yeow, J., Chia, C.G., Lim, N.Z. et al. J Am Chem Soc (2025) 147:24299-24308. DOI 10.1021/jacs.4c18050 · 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
- 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
- 8ODT 4.2 Å, Structure of TolQR complex from E.coli
Browse structure collections
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