8ODT: TolQR complex from E.coli

Structure of TolQR complex from E.coli. Determined by electron microscopy at 4.2 Å resolution. Released 1 Nov 2023.

Method: Electron microscopy
Resolution: 4.2 Å
Organism: Escherichia coli K-12
Chains: 7
Atoms: 9,304
Mol. weight: 169.32 kDa
Released: 1 Nov 2023

Explore 8ODT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ODT contains 45 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: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	6-11	6
α-helix	15-56	42
α-helix	62-71	10
α-helix	73-75	3
α-helix	78-97	20
α-helix	101-124	24
α-helix	127-156	30
α-helix	164-166	3
α-helix	168-228	61

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	7-12	6
α-helix	15-56	42
α-helix	62-70	9
α-helix	73-75	3
α-helix	78-96	19
α-helix	101-124	24
α-helix	127-156	30
α-helix	168-228	61

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	7-12	6
α-helix	15-56	42
α-helix	62-72	11
α-helix	73-75	3
α-helix	78-97	20
α-helix	101-124	24
α-helix	127-157	31
α-helix	168-227	60

Chain D: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	6-11	6
α-helix	15-56	42
α-helix	62-70	9
α-helix	73-75	3
α-helix	79-97	19
α-helix	101-124	24
α-helix	127-156	30
α-helix	164-166	3
α-helix	168-228	61

Chain E: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	6-12	7
α-helix	15-57	43
α-helix	62-70	9
α-helix	73-75	3
α-helix	79-97	19
α-helix	101-124	24
α-helix	127-156	30
α-helix	164-167	4
α-helix	168-228	61

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	25-34	10

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	21-34	14

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	189	Escherichia coli K-12	P0ABV6 (AlphaFold model)

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

>8ODT_1 Tol-Pal system protein TolQ (chains A, B, C, D, E)
MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGI
ELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNREL
ENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAI
GLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG

Sequence of entity 2 (F, G), FASTA

>8ODT_2 Tol-Pal system protein TolR (chains F, G)
MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSND
NPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEI
IKALNLLHSAGVKSVGLMTQPILEENLYFQGQFGSWSHPQFEKGGGSGGGSGGGSWSHPQ
FEKHHHHHH

Primary citation

Tunable force transduction through the Escherichia coli cell envelope. Williams-Jones, D.P., Webby, M.N., Press, C.E. et al. Proc Natl Acad Sci U S A (2023) 120:e2306707120-e2306707120. DOI 10.1073/pnas.2306707120 · 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
9KCH 4.19 Å, Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent…

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