7CH0: PDB entry 7CH0

The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation of E170Q on MlaF). Determined by electron microscopy at 3.7 Å resolution. Released 9 Sept 2020.

Method: Electron microscopy
Resolution: 3.7 Å
Organism: Escherichia coli K-12
Chains: 12
Atoms: 15,856
Mol. weight: 253.98 kDa
Ligands: ATP
Released: 9 Sept 2020

Explore 7CH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CH0 contains 91 α-helices and 108 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: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	4-31	28
α-helix	41-51	11
α-helix	53-55	3
α-helix	56-76	21
α-helix	79-81	3
α-helix	84-86	3
α-helix	88-94	7
α-helix	95-99	5
α-helix	100-125	26
α-helix	130-133	4
α-helix	139-142	4
α-helix	145-172	28
α-helix	173-177	5
α-helix	184-190	7
α-helix	195-200	6
α-helix	201-219	19
α-helix	228-242	15
α-helix	244-256	13

Chain B: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	14-18	5	2
β-strand	21-27	7	2
β-strand	30-32	3	1
β-strand	37-39	3	3
β-strand	40	1	4
α-helix	48-55	8
β-strand	65-67	3	1
β-strand	70-71	2	1
α-helix	77-83	7
β-strand	87-89	3	3
α-helix	103-106	4
α-helix	125-131	7
α-helix	149-156	8
β-strand	165-167	3	3
α-helix	183-188	6
β-strand	197-201	5	3
α-helix	208-210	3
β-strand	217-218	2	4
β-strand	223-225	3	4
α-helix	230-232	3
α-helix	262-265	4

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

Element	Residues	Length	Sheet
β-strand	6-9	4	9
β-strand	14-20	7	9
α-helix	26-30	5
β-strand	41-42	2	9
β-strand	46-50	5	9
α-helix	52-61	10
α-helix	63-67	5
α-helix	70-72	3
β-strand	73-74	2	9

Chain E: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	5
β-strand	14-18	5	6
β-strand	21-27	7	6
β-strand	30-32	3	5
β-strand	37-39	3	7
β-strand	40	1	8
α-helix	48-55	8
β-strand	65-67	3	5
β-strand	70-71	2	5
α-helix	77-83	7
β-strand	87-89	3	7
α-helix	103-106	4
α-helix	125-131	7
α-helix	149-156	8
β-strand	165-167	3	7
α-helix	183-188	6
β-strand	197-201	5	7
α-helix	208-210	3
β-strand	215-218	4	8
β-strand	223-227	5	8

Chain G: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	5-27	23
β-strand	39-45	7	11
β-strand	58-61	4	11
β-strand	63-70	8	11
α-helix	72	1
β-strand	73	1	12
α-helix	74	1
β-strand	80	1	12
β-strand	81-87	7	11
β-strand	98-102	5	11
β-strand	111-115	5	11
α-helix	116-118	3
β-strand	133	1	11
α-helix	144-151	8

Chain H: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	6-23	18
β-strand	39-40	2	13
β-strand	42-45	4	14
α-helix	56-57	2
β-strand	58-60	3	15
β-strand	63-64	2	15
β-strand	66	1	13
β-strand	70	1	14
β-strand	73-74	2	16
β-strand	79-80	2	16
β-strand	81-83	3	14
β-strand	86-87	2	13
β-strand	94	1	17
β-strand	102-103	2	18
β-strand	110-111	2	18
β-strand	112-113	2	15
β-strand	127	1	17
β-strand	132-134	3	14
α-helix	139-141	3
α-helix	143-150	8

Chain I: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-27	19
β-strand	39-43	5	19
β-strand	58-60	3	19
β-strand	63-68	6	19
β-strand	73	1	20
β-strand	80	1	20
β-strand	83-87	5	19
β-strand	94	1	21
β-strand	98-101	4	19
β-strand	112-115	4	19
α-helix	125-126	2
β-strand	127	1	21
α-helix	128	1
β-strand	133	1	19
β-strand	136-138	3	19
α-helix	139-140	2
α-helix	143-150	8

Chain J: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	5-27	23
β-strand	39-45	7	22
β-strand	57-60	4	22
β-strand	63-70	8	22
α-helix	72	1
β-strand	73	1	23
α-helix	74	1
β-strand	80	1	23
β-strand	81-87	7	22
β-strand	98-100	3	22
β-strand	103	1	24
β-strand	110	1	24
β-strand	113-115	3	22
β-strand	132-133	2	22
α-helix	139-142	4
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 K-12	P64606 (AlphaFold model)
Phospholipid ABC transporter ATP-binding protein MlaF	B, E	protein	269	Escherichia coli K-12	P63386 (AlphaFold model)
Lipid asymmetry maintenance protein MlaB	C, F	protein	97	Escherichia coli K-12	P64602 (AlphaFold model)
Outer membrane lipid asymmetry maintenance protein MlaD	G, H, I, J, K, L	protein	183	Escherichia coli K-12	P64604 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7CH0_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, D)
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV
VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI
GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI
DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV
HSSLAVLGLDFVLTALMFGN

Sequence of entity 2 (B, E), FASTA

>7CH0_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains B, E)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDQPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS

Sequence of entity 3 (C, F), FASTA

>7CH0_3 Lipid asymmetry maintenance protein MlaB (chains C, F)
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH
LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR

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

>7CH0_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
7CH7 3.9 Å, Cryo-EM structure of E.coli MlaFEB
6ZY4 4.1 Å, Cryo-EM structure of MlaFEDB in complex with ADP
7CGN 4.3 Å, The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation…

Browse structure collections

About this viewer

MolViewer shows 7CH0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.