8qp5

Release Complex: BAM bound EspP (SurA released)

Method: ELECTRON MICROSCOPY Dmax: 132.0 Å Quality: GOOD

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

Outer membrane protein assembly factor BamA

Escherichia coli

UniProt P0A940

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 21–810 Mutation:S425C Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA,Serine protease EspP × 1 (P0ABZ6,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

64 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–790; UniProt 21–810

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 20–392 Mutation:S425C Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA,Serine protease EspP × 1 (P0ABZ6,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 1–373; UniProt 20–392

Outer membrane protein assembly factor BamC

Escherichia coli

UniProt P0A903

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 25–344 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA,Serine protease EspP × 1 (P0ABZ6,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

51 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–320; UniProt 25–344

Outer membrane protein assembly factor BamD

Escherichia coli

UniProt P0AC02

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 20–245 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamE × 1 (P0A937) Chaperone SurA,Serine protease EspP × 1 (P0ABZ6,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–226; UniProt 20–245

Outer membrane protein assembly factor BamE

Escherichia coli

UniProt P0A937

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 20–113 Not recorded Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Chaperone SurA,Serine protease EspP × 1 (P0ABZ6,Q7BSW5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

46 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAME_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–94; UniProt 20–113

Chaperone SurA,Serine protease EspP

Escherichia coli

UniProt P0ABZ6

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 P; UniProt 21–428 Mutation:S1299C Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SURA_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain P; PDBConstruct 43–450; UniProt 21–428

Chaperone SurA,Serine protease EspP

Escherichia coli

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 P; UniProt 948–1300 Mutation:S1299C Outer membrane protein assembly factor BamA × 1 (P0A940) Outer membrane protein assembly factor BamB × 1 (P77774) Outer membrane protein assembly factor BamC × 1 (P0A903) Outer membrane protein assembly factor BamD × 1 (P0AC02) Outer membrane protein assembly factor BamE × 1 (P0A937) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 P; PDBConstruct 453–814; UniProt 948–1300

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 8qp5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qp5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qp5
Deposition date deposition_date2023-09-29
最后修订 last_revision2024-09-25
Structure title titleRelease Complex: BAM bound EspP (SurA released)
Keywords keywordsOuter Membrane, Complex, Chaperone, Protein Folding, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.32
Radius of gyration Rg (electron density) rg_electron45.77
Forward intensity I(0) i0511103000.00
Molecular weight molecular_weight177520.0 kDa
Excluded volume excluded_volume218290 ų
Envelope volume envelope_volume343570 ų
Hydration-shell volume shell_volume63590 ų
Envelope diameter envelope_diameter134.4
Shell Rg shell_rg49.90
Envelope Rg envelope_rg43.70
Shape Rg shape_rg45.77
Total Rg total_rg45.95
Total atoms total_atoms12549
Residues n_residues1746
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 dmax132.0
Rg (real space) rg_real46.04
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real5.1110e+08
I(0) uncertainty (real space) i0_real_error8.2380e+06
Rg (reciprocal space) rg_reciprocal46.31
I(0) (reciprocal space) i0_reciprocal511300000.0000
Solution quality estimate total_estimate0.8512
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.9
Skewness Skewness skewness-0.047
Kurtosis Kurtosis kurtosis-0.803
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52260000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.118

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)