8OJ4: MlaCD complex
Structure of the MlaCD complex (1:6 stoichiometry). Determined by electron microscopy at 4.35 Å resolution. Released 10 Jul 2024.
- Method
- Electron microscopy
- Resolution
- 4.35 Å
- Organism
- Escherichia coli
- Chains
- 7
- Atoms
- 6,983
- Mol. weight
- 141.55 kDa
- Released
- 10 Jul 2024
Explore 8OJ4 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8OJ4 contains 21 α-helices and 61 β-strands across 7 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: 1 helix, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 2 |
| β-strand | 60 | 1 | 3 |
| β-strand | 63 | 1 | 3 |
| β-strand | 66-73 | 8 | 2 |
| β-strand | 80-87 | 8 | 2 |
| β-strand | 98-103 | 6 | 4 |
| β-strand | 110-115 | 6 | 4 |
| β-strand | 120 | 1 | 5 |
| β-strand | 124 | 1 | 5 |
| β-strand | 133 | 1 | 2 |
| α-helix | 143-149 | 7 | |
Chain B: 2 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 40-45 | 6 | 6 |
| α-helix | 52-53 | 2 | |
| β-strand | 57-60 | 4 | 6 |
| β-strand | 63-73 | 11 | 6 |
| β-strand | 80-86 | 7 | 6 |
| β-strand | 97-103 | 7 | 6 |
| β-strand | 110-116 | 7 | 6 |
| β-strand | 133 | 1 | 6 |
| α-helix | 143-150 | 8 | |
Chain C: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 7 |
| α-helix | 52-53 | 2 | |
| β-strand | 58-60 | 3 | 8 |
| β-strand | 63-64 | 2 | 8 |
| β-strand | 66-73 | 8 | 7 |
| β-strand | 80-87 | 8 | 7 |
| β-strand | 94 | 1 | 9 |
| β-strand | 97-103 | 7 | 8 |
| β-strand | 110-116 | 7 | 8 |
| β-strand | 120 | 1 | 10 |
| β-strand | 124 | 1 | 10 |
| β-strand | 127 | 1 | 9 |
| β-strand | 133 | 1 | 7 |
| α-helix | 143-149 | 7 | |
Chain D: 1 helix, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 11 |
| β-strand | 57-60 | 4 | 12 |
| β-strand | 63-67 | 5 | 12 |
| β-strand | 68-72 | 5 | 11 |
| β-strand | 81-87 | 7 | 11 |
| β-strand | 98-103 | 6 | 12 |
| β-strand | 110-115 | 6 | 12 |
| β-strand | 132-133 | 2 | 11 |
| α-helix | 145-149 | 5 | |
Chain E: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 40-45 | 6 | 13 |
| β-strand | 57-60 | 4 | 13 |
| β-strand | 63-72 | 10 | 13 |
| β-strand | 81-86 | 6 | 13 |
| β-strand | 94 | 1 | 14 |
| β-strand | 98-102 | 5 | 13 |
| β-strand | 111-115 | 5 | 13 |
| β-strand | 120 | 1 | 15 |
| β-strand | 124 | 1 | 15 |
| β-strand | 127 | 1 | 14 |
| α-helix | 128-129 | 2 | |
| β-strand | 133 | 1 | 13 |
| α-helix | 145-149 | 5 | |
Chain F: 1 helix, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 16 |
| β-strand | 57-60 | 4 | 17 |
| β-strand | 63-67 | 5 | 17 |
| β-strand | 68-72 | 5 | 16 |
| β-strand | 81-87 | 7 | 16 |
| β-strand | 97-103 | 7 | 17 |
| β-strand | 110-116 | 7 | 17 |
| β-strand | 133 | 1 | 16 |
| β-strand | 137 | 1 | 17 |
| α-helix | 145-149 | 5 | |
Chain H: 12 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-43 | 17 | |
| α-helix | 47-51 | 5 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-62 | 7 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68 | 1 | 1 |
| α-helix | 71-74 | 4 | |
| α-helix | 80-84 | 5 | |
| α-helix | 87-108 | 22 | |
| α-helix | 119-122 | 4 | |
| β-strand | 130-135 | 6 | 1 |
| β-strand | 148-153 | 6 | 1 |
| β-strand | 162-163 | 2 | 1 |
| α-helix | 175-180 | 6 | |
| α-helix | 183-187 | 5 | |
| α-helix | 190-196 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Intermembrane phospholipid transport system binding protein MlaC | H | protein | 211 | Escherichia coli | P0ADV7 (AlphaFold model) |
| Intermembrane phospholipid transport system binding protein MlaD | A, B, C, D, E, F | protein | 183 | Escherichia coli | P64604 (AlphaFold model) |
Sequence of entity 1 (H), FASTA
>8OJ4_1 Intermembrane phospholipid transport system binding protein MlaC (chains H)
MFKRLMMVALLVIAPLSAATAADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIV
DQELLPYVQVKYAGALVLGQYYKSATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIA
PEQPLGDKTIVPIRVTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNE
WGTLLRTKGIDGLTAQLKSISQQKITLEEKK
Sequence of entity 2 (A, B, C, D, E, F), FASTA
>8OJ4_2 Intermembrane phospholipid transport system binding protein MlaD (chains A, B, C, D, E, F)
MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSI
GGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFED
PELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVG
TTK
Primary citation
Structure of the MlaC-MlaD complex reveals molecular basis of periplasmic phospholipid transport. Wotherspoon, P., Johnston, H., Hardy, D.J. et al. Nat Commun (2024) 15:6394-6394. DOI 10.1038/s41467-024-50615-3 · PubMed
Other PDB entries of the same protein (UniProt P0ADV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5UWA 1.5 Å, Structure of E. coli phospholipid binding protein MlaC
- 6GKI 2.23 Å, Structure of E coli MlaC in Variously Loaded States
- 7VR6 2.5 Å, Crystal structure of MlaC from Escherichia coli in quasi-open state
- 8I8X 3.25 Å, Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs
- 8OJG 4.38 Å, Structure of the MlaCD complex (2:6 stoichiometry)
Browse structure collections
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