8sqa

The cryo-EM structure of the EcBAM/EspP(beta8-12) complex

Method: ELECTRON MICROSCOPY Dmax: 135.4 Å Quality: GOOD

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

Outer membrane protein assembly factor BamA

Escherichia coli

UniProt C3TPJ2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 25–810 Not recorded Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator × 1 (P0AEY0,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3TPJ2_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–786; UniProt 25–810

Outer membrane protein assembly factor BamB

Escherichia coli

UniProt P77774

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 21–392 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator × 1 (P0AEY0,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

63 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMB_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–372; UniProt 21–392

Outer membrane protein assembly factor BamC

Escherichia coli

UniProt C3T0D3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 27–345 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator × 1 (P0AEY0,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3T0D3_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–319; UniProt 27–345

Outer membrane protein assembly factor BamD

Escherichia coli

UniProt C3SYV7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 21–245 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator × 1 (P0AEY0,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SYV7_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–225; UniProt 21–245

Outer membrane protein assembly factor BamE

Escherichia coli

UniProt A0A366UU94

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 21–113 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator × 1 (P0AEY0,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

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

View Construct and Data Evidence
UniProt name A0A366UU94_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–93; UniProt 21–113

Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator

Escherichia coli O157

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 26–392 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 3–369; UniProt 26–392

Maltose/maltodextrin-binding periplasmic protein,Autotransporter protein EspP translocator

Escherichia coli O157

UniProt Q7BSW5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1195–1300 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (C3T0D3) Outer membrane protein assembly factor BamD × 1 (C3SYV7) Outer membrane protein assembly factor BamE × 1 (A0A366UU94) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ESPP_ECO57
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 446–551; UniProt 1195–1300

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 8sqa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sqa
Deposition date deposition_date2023-05-04
Structure title titleThe cryo-EM structure of the EcBAM/EspP(beta8-12) complex
Keywords keywordsmembrane proteins, protein folding, BAM complex, outer membrane protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.33
Radius of gyration Rg (electron density) rg_electron42.93
Forward intensity I(0) i0456364000.00
Molecular weight molecular_weight172160.0 kDa
Excluded volume excluded_volume214200 ų
Envelope volume envelope_volume320500 ų
Hydration-shell volume shell_volume63444 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg47.65
Envelope Rg envelope_rg40.94
Shape Rg shape_rg42.92
Total Rg total_rg43.19
Total atoms total_atoms12156
Residues n_residues1563
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 dmax135.4
Rg (real space) rg_real43.11
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real4.5640e+08
I(0) uncertainty (real space) i0_real_error7.4130e+06
Rg (reciprocal space) rg_reciprocal43.33
I(0) (reciprocal space) i0_reciprocal456500000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.9
Skewness Skewness skewness0.030
Kurtosis Kurtosis kurtosis-0.630
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45420000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)