7CGE: PDB entry 7CGE
The overall structure of nucleotide free MlaFEDB complex. Determined by electron microscopy at 2.9 Å resolution. Released 9 Sept 2020.
- Method
- Electron microscopy
- Resolution
- 2.9 Å
- Organism
- Escherichia coli (strain K12)
- Chains
- 12
- Atoms
- 16,406
- Mol. weight
- 261.96 kDa
- Ligands
- PGW
- Released
- 9 Sept 2020
Explore 7CGE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7CGE contains 73 α-helices and 105 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.
Chain A: 15 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-31 | 26 | |
| α-helix | 41-50 | 10 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-78 | 23 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-96 | 10 | |
| α-helix | 100-125 | 26 | |
| α-helix | 128-133 | 6 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-174 | 30 | |
| α-helix | 182-190 | 9 | |
| α-helix | 195-200 | 6 | |
| α-helix | 201-222 | 22 | |
| α-helix | 228-257 | 30 | |
Chains B and E: 9 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-14 | 8 | 1 |
| β-strand | 15 | 1 | 2 |
| β-strand | 16-18 | 3 | 1 |
| β-strand | 21-32 | 12 | 1 |
| β-strand | 36-40 | 5 | 3 |
| α-helix | 50-54 | 5 | |
| β-strand | 62 | 1 | 2 |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 70-71 | 2 | 1 |
| α-helix | 77-83 | 7 | |
| β-strand | 87-90 | 4 | 3 |
| α-helix | 102-106 | 5 | |
| α-helix | 122-131 | 10 | |
| α-helix | 142-144 | 3 | |
| α-helix | 150-156 | 7 | |
| β-strand | 165-169 | 5 | 3 |
| α-helix | 177-192 | 16 | |
| β-strand | 197-202 | 6 | 3 |
| α-helix | 205-208 | 4 | |
| β-strand | 214-217 | 4 | 3 |
| β-strand | 225-227 | 3 | 3 |
| α-helix | 238-245 | 8 | |
Chains C and F: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 4 |
| β-strand | 13 | 1 | 5 |
| β-strand | 14-20 | 7 | 4 |
| α-helix | 26-29 | 4 | |
| β-strand | 41-42 | 2 | 5 |
| β-strand | 46-50 | 5 | 4 |
| α-helix | 52-67 | 16 | |
| β-strand | 73-74 | 2 | 5 |
| α-helix | 81-87 | 7 | |
Chain D: 15 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-31 | 26 | |
| α-helix | 41-51 | 11 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-78 | 23 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-96 | 10 | |
| α-helix | 100-125 | 26 | |
| α-helix | 128-133 | 6 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-174 | 30 | |
| α-helix | 182-190 | 9 | |
| α-helix | 195-200 | 6 | |
| α-helix | 201-222 | 22 | |
| α-helix | 228-257 | 30 | |
Chain G: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-23 | 19 | |
| α-helix | 24-28 | 5 | |
| β-strand | 39-43 | 5 | 11 |
| β-strand | 58-60 | 3 | 11 |
| β-strand | 63-68 | 6 | 11 |
| β-strand | 83-87 | 5 | 11 |
| β-strand | 94 | 1 | 12 |
| β-strand | 98 | 1 | 13 |
| β-strand | 101-102 | 2 | 11 |
| β-strand | 111-113 | 3 | 11 |
| β-strand | 115 | 1 | 13 |
| β-strand | 127 | 1 | 12 |
| β-strand | 133 | 1 | 11 |
| α-helix | 144-151 | 8 | |
Chain H: 2 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-27 | 21 | |
| β-strand | 39-45 | 7 | 14 |
| β-strand | 58-60 | 3 | 15 |
| β-strand | 63-66 | 4 | 15 |
| β-strand | 68 | 1 | 14 |
| β-strand | 73-74 | 2 | 16 |
| β-strand | 79-80 | 2 | 16 |
| β-strand | 81-87 | 7 | 14 |
| β-strand | 98-102 | 5 | 15 |
| β-strand | 111-115 | 5 | 15 |
| β-strand | 132-134 | 3 | 14 |
| α-helix | 145-150 | 6 | |
Chain I: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-26 | 21 | |
| β-strand | 39-45 | 7 | 17 |
| β-strand | 58-60 | 3 | 17 |
| β-strand | 63-68 | 6 | 17 |
| β-strand | 73-74 | 2 | 18 |
| β-strand | 79-80 | 2 | 18 |
| β-strand | 81-87 | 7 | 17 |
| β-strand | 94 | 1 | 19 |
| β-strand | 98-102 | 5 | 17 |
| β-strand | 111-115 | 5 | 17 |
| α-helix | 125-126 | 2 | |
| β-strand | 127 | 1 | 19 |
| α-helix | 128 | 1 | |
| β-strand | 133-134 | 2 | 17 |
| α-helix | 144-151 | 8 | |
Chain J: 4 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-23 | 19 | |
| α-helix | 24-28 | 5 | |
| β-strand | 39-40 | 2 | 20 |
| β-strand | 42-45 | 4 | 20 |
| β-strand | 58-60 | 3 | 20 |
| β-strand | 63-69 | 7 | 20 |
| α-helix | 72 | 1 | |
| β-strand | 73-74 | 2 | 21 |
| β-strand | 79-80 | 2 | 21 |
| β-strand | 81-87 | 7 | 20 |
| β-strand | 94 | 1 | 22 |
| β-strand | 101-102 | 2 | 20 |
| β-strand | 111-113 | 3 | 20 |
| β-strand | 127 | 1 | 22 |
| β-strand | 132-134 | 3 | 20 |
| α-helix | 144-151 | 8 | |
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
>7CGE_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, D)
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV
VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI
GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI
DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV
HSSLAVLGLDFVLTALMFGN
Sequence of entity 2 (B, E), FASTA
>7CGE_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains B, E)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS
Sequence of entity 3 (C, F), FASTA
>7CGE_3 Lipid asymmetry maintenance protein MlaB (chains C, F)
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH
LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR
Sequence of entity 4 (G, H, I, J, K, L), FASTA
>7CGE_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 |
|---|
| PGW | (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade… | C40 H77 O10 P | 12 |
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:
- 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
- 7CGN 4.3 Å, The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation…
Browse structure collections
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