1L7V: Bacterial ABC Transporter Involved in B12 Uptake

Bacterial ABC Transporter Involved in B12 Uptake. Determined by X-ray diffraction at 3.2 Å resolution. Released 15 May 2002.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Escherichia coli
Chains: 4
Atoms: 8,410
Mol. weight: 126.84 kDa
Ligands: V4O
Released: 15 May 2002

Explore 1L7V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L7V contains 57 α-helices and 34 β-strands across 4 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: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-32	30
β-strand	33	1	1
β-strand	37	1	1
α-helix	41-43	3
α-helix	49-56	8
α-helix	57-81	25
α-helix	93-106	14
α-helix	114-138	25
α-helix	142-167	26
α-helix	172-179	8
α-helix	188-190	3
α-helix	191-206	16
α-helix	208-216	9
α-helix	218-223	6
α-helix	228-250	23
α-helix	259-266	8
α-helix	272-296	25
α-helix	305-323	19

Chain B: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	3-32	30
α-helix	46-48	3
α-helix	49-56	8
α-helix	57-80	24
α-helix	88-91	4
α-helix	93-107	15
α-helix	114-138	25
α-helix	142-167	26
α-helix	172-179	8
α-helix	188-190	3
α-helix	191-204	14
α-helix	208-216	9
α-helix	218-223	6
α-helix	228-250	23
α-helix	259-266	8
α-helix	272-296	25
α-helix	305-323	19

Chains C and D: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	2
β-strand	19-24	6	2
β-strand	28-30	3	3
β-strand	32	1	4
α-helix	39-47	9
β-strand	55-58	4	2
β-strand	62	1	2
α-helix	63-65	3
α-helix	68-74	7
β-strand	75-78	4	3
α-helix	83-85	3
β-strand	89	1	5
α-helix	90-97	8
α-helix	104-113	10
β-strand	123	1	5
α-helix	124-126	3
α-helix	129-144	16
β-strand	154-157	4	3
α-helix	166-181	16
β-strand	185-188	4	3
α-helix	193-199	7
β-strand	202	1	3
β-strand	205	1	4
β-strand	206-208	3	6
β-strand	210-211	2	6
β-strand	216	1	3
α-helix	217-220	4
α-helix	223-230	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vitamin B12 transport system permease protein btuc	A, B	protein	326	Escherichia coli	P06609 (AlphaFold model)
Vitamin B12 transport ATP-binding protein btuD	C, D	protein	249	Escherichia coli	P06611 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1L7V_1 VITAMIN B12 TRANSPORT SYSTEM PERMEASE PROTEIN BTUC (chains A, B)
MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWISPGDWFTPRGELFVWQIRLPRT
LAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLC
AIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMM
GGFGGVDWRQSWLMLALIPVLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATG
WMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAA
AELPIGVVTATLGAPVFIWLLLKAGR

Sequence of entity 2 (C, D), FASTA

>1L7V_2 Vitamin B12 transport ATP-binding protein btuD (chains C, D)
MSIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAG
QPLEAWSATKLALHRAYLSQQQTPPFATPVWHYLTLHQHDKTRTELLNDVAGALALDDKL
GRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEPMNSLDVAQQSALDKILSALC
QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIE
GHRMLISTI

Ligands and cofactors

ID	Name	Formula	Copies
V4O	Cyclo-tetrametavanadate	O12 V4	2

Primary citation

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Locher, K.P., Lee, A.T., Rees, D.C. Science (2002) 296:1091-1098. DOI 10.1126/science.1071142 · PubMed

Other PDB entries of the same protein (UniProt P06609 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2QI9 2.6 Å, ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF
4R9U 2.79 Å, Structure of vitamin B12 transporter BtuCD in a nucleotide-bound outward facing state
4FI3 3.47 Å, Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state
4DBL 3.49 Å, Crystal structure of E159Q mutant of BtuCDF

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1L7V is part of these collections:

Membrane proteins and transporters

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