8i8x

Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs

Method: ELECTRON MICROSCOPY Dmax: 145.3 Å Quality: GOOD

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

Outer membrane porin C

Escherichia coli K-12

UniProt P06996

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 22–367 Chain B; UniProt 22–367 Chain C; UniProt 22–367 Not recorded Intermembrane phospholipid transport system lipoprotein MlaA × 1 (P76506) Intermembrane phospholipid transport system binding protein MlaC × 1 (P0ADV7) 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

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OMPC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–346; UniProt 22–367 Author chain B; PDBConstruct 1–346; UniProt 22–367 Author chain C; PDBConstruct 1–346; UniProt 22–367

Intermembrane phospholipid transport system lipoprotein MlaA

Escherichia coli K-12

UniProt P76506

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 18–251 Mutation:Q205C Outer membrane porin C × 3 (P06996) Intermembrane phospholipid transport system binding protein MlaC × 1 (P0ADV7) 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

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLAA_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–234; UniProt 18–251

Intermembrane phospholipid transport system binding protein MlaC

Escherichia coli K-12

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 21–211 Mutation:V171C Outer membrane porin C × 3 (P06996) Intermembrane phospholipid transport system lipoprotein MlaA × 1 (P76506) 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

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.

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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–191; UniProt 21–211

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 8i8x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i8x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i8x
Deposition date deposition_date2023-02-05
Structure title titleCryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs
Keywords keywordsbacteria, outer membrane, phospholipid, lipid asymmetry, membrane protein, protein complex structure, channel, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.24
Radius of gyration Rg (electron density) rg_electron40.74
Forward intensity I(0) i0405048000.00
Molecular weight molecular_weight158570.0 kDa
Excluded volume excluded_volume195640 ų
Envelope volume envelope_volume292220 ų
Hydration-shell volume shell_volume60678 ų
Envelope diameter envelope_diameter155.2
Shell Rg shell_rg45.05
Envelope Rg envelope_rg41.90
Shape Rg shape_rg40.81
Total Rg total_rg40.79
Total atoms total_atoms11226
Residues n_residues1450
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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 dmax145.3
Rg (real space) rg_real41.53
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real4.0500e+08
I(0) uncertainty (real space) i0_real_error7.4440e+06
Rg (reciprocal space) rg_reciprocal41.25
I(0) (reciprocal space) i0_reciprocal404900000.0000
Solution quality estimate total_estimate0.8294
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.1
Skewness Skewness skewness0.608
Kurtosis Kurtosis kurtosis-0.056
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53860000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.671; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)