2HQS: TolB/Pal complex

Crystal structure of TolB/Pal complex. Determined by X-ray diffraction at 1.5 Å resolution. Released 3 Apr 2007.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Escherichia coli
Chains: 8
Atoms: 18,839
Mol. weight: 233.58 kDa
Released: 3 Apr 2007

Explore 2HQS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HQS contains 60 α-helices and 144 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: 9 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	27-30	4	1
β-strand	36-38	3	2
β-strand	39-40	2	3
α-helix	41-43	3
β-strand	44-45	2	3
α-helix	55-65	11
β-strand	69-71	3	2
α-helix	72-73	2
α-helix	74-76	3
α-helix	84-86	3
α-helix	89-93	5
β-strand	99-107	9	3
β-strand	113-121	9	3
β-strand	129-137	9	3
α-helix	139-141	3
α-helix	142-158	17
β-strand	167-173	7	4
β-strand	181-187	7	4
β-strand	194-199	6	4
β-strand	203-208	6	5
β-strand	214-219	6	5
β-strand	226-231	6	5
β-strand	237-241	5	5
β-strand	247-252	6	6
β-strand	258-263	6	6
β-strand	270-275	6	6
β-strand	281-283	3	6
β-strand	291-296	6	7
β-strand	302-307	6	7
β-strand	314-319	6	7
β-strand	326-327	2	7
β-strand	334-340	7	8
β-strand	346-352	7	8
β-strand	357-363	7	8
β-strand	369-371	3	8
β-strand	379-383	5	1
β-strand	389-396	8	1
β-strand	399-406	8	1
β-strand	412-414	3	1
β-strand	421-427	7	4
α-helix	428-431	4

Chain B: 9 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	27-30	4	10
β-strand	36-38	3	11
β-strand	39-40	2	12
α-helix	41-43	3
β-strand	44-45	2	12
α-helix	55-65	11
β-strand	69-71	3	11
α-helix	72-73	2
α-helix	74-76	3
α-helix	84-86	3
α-helix	89-93	5
β-strand	99-107	9	12
β-strand	113-121	9	12
β-strand	129-137	9	12
α-helix	139-141	3
α-helix	142-158	17
β-strand	167-173	7	13
β-strand	181-187	7	13
β-strand	194-199	6	13
β-strand	203-208	6	14
β-strand	214-219	6	14
β-strand	226-231	6	14
β-strand	237-241	5	14
β-strand	247-252	6	15
β-strand	258-263	6	15
β-strand	270-275	6	15
β-strand	281-283	3	15
β-strand	291-296	6	16
β-strand	302-307	6	16
β-strand	314-319	6	16
β-strand	326-327	2	16
β-strand	334-340	7	17
β-strand	346-353	8	17
β-strand	356-363	8	17
β-strand	369-371	3	17
β-strand	379-383	5	10
β-strand	389-396	8	10
β-strand	399-406	8	10
β-strand	412-414	3	10
β-strand	421-427	7	13
α-helix	428-430	3

Chains C and E: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	70-72	3	18
α-helix	82-84	3
α-helix	85-97	13
β-strand	103-107	5	18
α-helix	115-135	21
α-helix	140-142	3
β-strand	143-147	5	18
α-helix	160-166	7
β-strand	168-172	5	18

Chains D and F: 10 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	27-30	4	19
α-helix	32-34	3
β-strand	36-38	3	20
β-strand	39-40	2	21
α-helix	41-43	3
β-strand	44-45	2	21
α-helix	55-65	11
β-strand	69-71	3	20
α-helix	72-73	2
α-helix	74-76	3
α-helix	84-86	3
α-helix	89-93	5
β-strand	99-107	9	21
β-strand	113-121	9	21
β-strand	129-137	9	21
α-helix	139-141	3
α-helix	142-158	17
β-strand	167-173	7	22
β-strand	181-187	7	22
β-strand	194-199	6	22
β-strand	203-208	6	23
β-strand	214-219	6	23
β-strand	226-231	6	23
β-strand	237-241	5	23
β-strand	247-252	6	24
β-strand	258-263	6	24
β-strand	270-275	6	24
β-strand	281-283	3	24
β-strand	291-296	6	25
β-strand	302-307	6	25
β-strand	314-319	6	25
β-strand	326-327	2	25
β-strand	335-340	6	26
β-strand	346-353	8	26
β-strand	356-363	8	26
β-strand	369-371	3	26
β-strand	379-383	5	19
β-strand	389-396	8	19
β-strand	399-406	8	19
β-strand	412-414	3	19
β-strand	421-427	7	22
α-helix	428-430	3

Chains G and H: 6 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	70-72	3	36
α-helix	79-81	3
α-helix	82-84	3
α-helix	85-97	13
β-strand	103-107	5	36
α-helix	115-135	21
α-helix	140-142	3
β-strand	143-147	5	36
α-helix	160-166	7
β-strand	168-172	5	36

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein tolB	A, B, D, F	protein	415	Escherichia coli	P0A855 (AlphaFold model)
Peptidoglycan-associated lipoprotein	C, E, G, H	protein	118	Escherichia coli	P0A912 (AlphaFold model)

Sequence of entity 1 (A, B, D, F), FASTA

>2HQS_1 Protein tolB (chains A, B, D, F)
MVRIVIDSGVDSGRPIGVVPFQWAGPGAAPEDIGGIVAADLRNSGKFNPLDRARLPQQPG
SAQEVQPAAWSALGIDAVVVGQVTPNPDGSYNVAYQLVDTGGAPGTVLAQNSYKVNKQWL
RYAGHTASDEVFEKLTGIKGAFRTRIAYVVQTNGGQFPYELRVSDYDGYNQFVVHRSPQP
LMSPAWSPDGSKLAYVTFESGRSALVIQTLANGAVRQVASFPRHNGAPAFSPDGSKLAFA
LSKTGSLNLYVMDLASGQIRQVTDGRSNNTEPTWFPDSQNLAFTSDQAGRPQVYKVNING
GAPQRITWEGSQNQDADVSSDGKFMVMVSSNGGQQHIAKQDLATGGVQVLSSTFLDETPS
LAPNGTMVIYSSSQGMGSVLNLVSTDGRFKARLPATDGQVKFPAWSPYLHHHHHH

Sequence of entity 2 (C, E, G, H), FASTA

>2HQS_2 Peptidoglycan-associated lipoprotein (chains C, E, G, H)
MLQQNNIVYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGE
RRANAVKMYLQGKGVSADQISIVSYGKEKPAVLGHDEAAYSKNRRAVLVYLEHHHHHH

Primary citation

Molecular mimicry enables competitive recruitment by a natively disordered protein. Bonsor, D.A., Grishkovskaya, I., Dodson, E.J. et al. J Am Chem Soc (2007) 129:4800-4807. DOI 10.1021/ja070153n · PubMed

Other PDB entries of the same protein (UniProt P0A855 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2W8B 1.86 Å, Crystal structure of processed TolB in complex with Pal
1CRZ 1.95 Å, Crystal structure of the E. Coli tolb protein
1C5K 2.0 Å, The structure of tolb, an essential component of the tol-dependent translocation system…
2IVZ 2.0 Å, Structure of TolB in complex with a peptide of the colicin E9 T- domain
4JML 2.0 Å, Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.
3IAX 2.6 Å, The crystal structure of the TolB box of Colicin A in complex with TolB reveals…
7NST 3.7 Å, ColicinE9 partial translocation complex
7NSU 4.7 Å, ColicinE9 intact translocation complex
9A2L Model of E. coli TolB by in-cell photo-crosslinking MS and deep learning

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