← Back to search
8ojg

Structure of the MlaCD complex (2:6 stoichiometry)

Method: ELECTRON MICROSCOPY Dmax: 107.1 Å Quality: GOOD
▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Intermembrane phospholipid transport system binding protein MlaD

Escherichia coli

UniProt P64604

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 1–183 Chain B； UniProt 1–183 Chain C； UniProt 1–183 Chain D； UniProt 1–183 Chain E； UniProt 1–183 Chain F； UniProt 1–183 Not recorded Intermembrane phospholipid transport system binding protein MlaC × 2 （P0ADV7） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.38 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8OJG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8HPZ Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form I) Deposited 2022-12-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 29–183（155 aa）
Chain B 29–183（155 aa）
Chain C 29–183（155 aa）
Not recorded CO2 CARBON DIOXIDE × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 5；293 K；1.8 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic pH 5.0
Resolution 2.30 Å R-free 0.273
8HQ9 Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form II) Deposited 2022-12-13 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 29–183（155 aa）
Chain B 29–183（155 aa）
Chain C 29–183（155 aa）
Chain D 29–183（155 aa）
Chain E 29–183（155 aa）
Chain F 29–183（155 aa）
Not recorded MG MAGNESIUM ION × 1 CO2 CARBON DIOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 5；293 K；0.2 M magnesium chloride hexahydrate, 0.1 M sodium citrate tribasic dihyrate pH 5.0, 10% (w/v) PEG 20000
Resolution 2.70 Å R-free 0.261
8HQA Crystal structure of the ectodomain of the MlaD protein from Escherichia coli in the resting state Deposited 2022-12-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 29–183（155 aa）
Chain B 29–183（155 aa）
Chain C 29–183（155 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8.5；293 K；0.01 M nickel(II) chloride hexahydrate, 0.1 M tris pH 8.5, 20% (w/v) PEG monoethyl ether 2000
Resolution 3.20 Å R-free 0.275
8OJ4 Structure of the MlaCD complex (1:6 stoichiometry) Deposited 2023-03-23 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.35 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLAD_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–183； UniProt 1–183 Author chain B； PDBConstruct 1–183； UniProt 1–183 Author chain C； PDBConstruct 1–183； UniProt 1–183 Author chain D； PDBConstruct 1–183； UniProt 1–183 Author chain E； PDBConstruct 1–183； UniProt 1–183 Author chain F； PDBConstruct 1–183； UniProt 1–183

Intermembrane phospholipid transport system binding protein MlaC

Escherichia coli

UniProt P0ADV7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain G； UniProt 1–211 Chain H； UniProt 1–211 Not recorded Intermembrane phospholipid transport system binding protein MlaD × 6 （P64604） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.38 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8OJG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5UWA Structure of E. coli phospholipid binding protein MlaC Deposited 2017-02-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–211（190 aa）
Not recorded 8ND (2S)-3-(2-aminoethoxy)propane-1,2-diyl dihexadecanoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M citric acid pH 3.5 and 1.6 M ammonium sulfate
Resolution 1.50 Å R-free 0.168
5UWA Structure of E. coli phospholipid binding protein MlaC Deposited 2017-02-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 22–211（190 aa）
Not recorded 8ND (2S)-3-(2-aminoethoxy)propane-1,2-diyl dihexadecanoate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M citric acid pH 3.5 and 1.6 M ammonium sulfate
Resolution 1.50 Å R-free 0.168
6GKI Structure of E coli MlaC in Variously Loaded States Deposited 2018-05-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–211（190 aa）
Not recorded BR BROMIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；seed grown in (0.1M Na Cacodylate pH 6.5, 2M ammonium sulphate, 0.2M NaCl) seed transferred to drop of (0.09M NaF/Br/I, 0.1M Tris/bicine pH 8.5, 20% glycerol, 10% PEG 4000)
Resolution 2.23 Å R-free 0.236
6GKI Structure of E coli MlaC in Variously Loaded States Deposited 2018-05-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 22–211（190 aa）
Not recorded BR BROMIDE ION × 4 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；seed grown in (0.1M Na Cacodylate pH 6.5, 2M ammonium sulphate, 0.2M NaCl) seed transferred to drop of (0.09M NaF/Br/I, 0.1M Tris/bicine pH 8.5, 20% glycerol, 10% PEG 4000)
Resolution 2.23 Å R-free 0.236
7VR6 Crystal structure of MlaC from Escherichia coli in quasi-open state Deposited 2021-10-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 22–211（190 aa）
Not recorded PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.7 M sodium citrate tribasic dihydrate, 0.1 M Bis-Tris propane pH 7.0
Resolution 2.50 Å R-free 0.217
8I8X Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs Deposited 2023-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain F 21–211（191 aa）
Mutation：V171C KDL (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；Tris-buffered saline (TBS) buffer (20 mM Tris HCl pH 8.0, 150 mM NaCl)
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.25 Å
8OJ4 Structure of the MlaCD complex (1:6 stoichiometry) Deposited 2023-03-23 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain H 1–211（211 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.35 Å

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLAC_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain G； PDBConstruct 1–211； UniProt 1–211 Author chain H； PDBConstruct 1–211； UniProt 1–211

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8ojg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ojg
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ojg
Deposition date deposition_date2023-03-24
Structure title titleStructure of the MlaCD complex (2:6 stoichiometry)
Keywords keywordsOuter membrane, phospholipids, gram-negative bacteria, lipid transport; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.24 Å
Radius of gyration Rg (electron density) rg_electron36.14 Å
Forward intensity I(0) i0208310000.00
Molecular weight molecular_weight117940.0 kDa
Excluded volume excluded_volume148830 ų
Envelope volume envelope_volume233720 ų
Hydration-shell volume shell_volume53236 ų
Envelope diameter envelope_diameter107.5 Å
Shell Rg shell_rg43.54 Å
Envelope Rg envelope_rg34.68 Å
Shape Rg shape_rg36.16 Å
Total Rg total_rg36.66 Å
Total atoms total_atoms8325
Residues n_residues1065
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax107.1 Å
Rg (real space) rg_real36.98 Å
Rg uncertainty (real space) rg_real_error0.50 Å
I(0) (real space) i0_real2.0830e+08
I(0) uncertainty (real space) i0_real_error3.1780e+06
Rg (reciprocal space) rg_reciprocal37.15 Å
I(0) (reciprocal space) i0_reciprocal208300000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.0 Å
Skewness Skewness skewness0.006
Kurtosis Kurtosis kurtosis-0.735
Angular range angular_range— – 0.2100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57910000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.656
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▶

8. Citations (1)

▶

9. Files and Curves (10)