7CGN: PDB entry 7CGN

The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation of E170Q on MlaF). Determined by electron microscopy at 4.3 Å resolution. Released 9 Sept 2020.

Method: Electron microscopy
Resolution: 4.3 Å
Organism: Escherichia coli (strain K12)
Chains: 12
Atoms: 15,854
Mol. weight: 253.98 kDa
Ligands: ATP
Released: 9 Sept 2020

Explore 7CGN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CGN contains 83 α-helices and 104 β-strands across 12 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.

Chains A and D: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	6-30	25
α-helix	40-48	9
α-helix	49-53	5
α-helix	56-79	24
α-helix	85-87	3
α-helix	88-94	7
α-helix	95-99	5
α-helix	100-108	9
α-helix	109-113	5
α-helix	114-125	12
α-helix	128-132	5
α-helix	139	1
α-helix	140-144	5
α-helix	145-152	8
α-helix	154-172	19
α-helix	173-177	5
α-helix	182-190	9
α-helix	195-199	5
α-helix	200-220	21
α-helix	228-257	30

Chain B: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-14	8	1
β-strand	27-32	6	1
β-strand	36-39	4	2
α-helix	47-55	9
β-strand	65-67	3	1
β-strand	71	1	1
α-helix	72-74	3
α-helix	77-83	7
β-strand	87-90	4	2
α-helix	102-106	5
α-helix	110-113	4
α-helix	118-131	14
α-helix	148-158	11
β-strand	165-169	5	2
α-helix	177-192	16
β-strand	197-201	5	2
α-helix	205-208	4
β-strand	214-216	3	2
β-strand	227-228	2	2
α-helix	238-245	8

Chains C and F: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	3
β-strand	14	1	3
α-helix	26-30	5
β-strand	41-42	2	3
α-helix	52-63	12
β-strand	73-74	2	3
α-helix	81-87	7

Chain E: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-14	8	4
β-strand	27-32	6	4
β-strand	36-40	5	5
α-helix	47-55	9
β-strand	65-67	3	4
β-strand	71	1	4
α-helix	72-74	3
α-helix	77-83	7
β-strand	87-90	4	5
α-helix	102-106	5
α-helix	110-113	4
α-helix	118-131	14
α-helix	148-158	11
β-strand	165-169	5	5
α-helix	177-192	16
β-strand	197-201	5	5
α-helix	205-208	4
β-strand	214-217	4	5
β-strand	227-228	2	5
α-helix	238-245	8

Chain G: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	5-22	18
α-helix	23-27	5
β-strand	39-45	7	7
β-strand	57-60	4	7
β-strand	63-68	6	7
β-strand	81-87	7	7
β-strand	94	1	8
β-strand	97-98	2	9
β-strand	101-102	2	7
β-strand	111-114	4	7
β-strand	115-116	2	9
β-strand	122	1	10
β-strand	124	1	10
β-strand	127	1	8
β-strand	133-134	2	7
α-helix	146-149	4

Chain H: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	10-27	18
β-strand	39-45	7	11
β-strand	57-60	4	12
β-strand	63-67	5	12
β-strand	68	1	11
β-strand	81-87	7	11
β-strand	94	1	13
β-strand	97-98	2	14
β-strand	101	1	12
β-strand	112-114	3	12
β-strand	115-116	2	14
β-strand	127	1	13
β-strand	133-134	2	11
α-helix	145-151	7

Chain I: 3 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	5-27	23
β-strand	39-40	2	15
β-strand	44	1	16
β-strand	45	1	17
β-strand	56-60	5	18
β-strand	63-68	6	18
β-strand	81	1	17
β-strand	84	1	18
β-strand	86-87	2	15
β-strand	94	1	19
β-strand	97-98	2	20
β-strand	101	1	18
β-strand	112-114	3	18
β-strand	115-116	2	20
α-helix	125-126	2
β-strand	127	1	19
β-strand	134	1	16
α-helix	143-151	9

Chain J: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	5-28	24
β-strand	39-45	7	21
α-helix	56	1
β-strand	57-60	4	22
β-strand	63-67	5	22
β-strand	81-87	7	21
β-strand	94	1	23
β-strand	97-98	2	24
β-strand	101	1	22
β-strand	112-114	3	22
β-strand	115-116	2	24
β-strand	127	1	23
β-strand	133-134	2	21
α-helix	143-151	9

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lipid asymmetry maintenance ABC transporter permease subunit MlaE	A, D	protein	260	Escherichia coli (strain K12)	P64606 (AlphaFold model)
Phospholipid ABC transporter ATP-binding protein MlaF	B, E	protein	269	Escherichia coli (strain K12)	P63386 (AlphaFold model)
Lipid asymmetry maintenance protein MlaB	C, F	protein	97	Escherichia coli (strain K12)	P64602 (AlphaFold model)
Outer membrane lipid asymmetry maintenance protein MlaD	G, H, I, J, K, L	protein	183	Escherichia coli (strain K12)	P64604 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7CGN_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, D)
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV
VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI
GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI
DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV
HSSLAVLGLDFVLTALMFGN

Sequence of entity 2 (B, E), FASTA

>7CGN_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains B, E)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDQPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS

Sequence of entity 3 (C, F), FASTA

>7CGN_3 Lipid asymmetry maintenance protein MlaB (chains C, F)
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH
LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR

Sequence of entity 4 (G, H, I, J, K, L), FASTA

>7CGN_4 Outer membrane lipid asymmetry maintenance protein MlaD (chains G, H, I, J, K, L)
MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSI
GGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFED
PELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVG
TTK

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Structural mechanism of phospholipids translocation by MlaFEDB complex. Chi, X., Fan, Q., Zhang, Y. et al. Cell Res (2020) 30:1127-1135. DOI 10.1038/s41422-020-00404-6 · PubMed

Other PDB entries of the same protein (UniProt P64606 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CGE 2.9 Å, The overall structure of nucleotide free MlaFEDB complex
6XBD 3.05 Å, Cryo-EM structure of MlaFEDB in nanodiscs with phospholipid substrates
6ZY3 3.3 Å, Cryo-EM structure of MlaFEDB in complex with phospholipid
6ZY9 3.3 Å, Cryo-EM structure of MlaFEDB in complex with AMP-PNP
7CH6 3.4 Å, Cryo-EM structure of E.coli MlaFEB with AMPPNP
6ZY2 3.6 Å, Cryo-EM structure of apo MlaFEDB
7CH0 3.7 Å, The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation…
7CH7 3.9 Å, Cryo-EM structure of E.coli MlaFEB
6ZY4 4.1 Å, Cryo-EM structure of MlaFEDB in complex with ADP

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