7tt5

BamABCDE bound to substrate EspP in the open-sheet EspP state

Method: ELECTRON MICROSCOPY Dmax: 124.6 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera

Escherichia coli

UniProt P0AEX9

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain P; UniProt 26–392 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamE × 1 (A0A3L5AP29) Outer membrane protein assembly factor BamD × 1 (A0A1X3I1M6) Outer membrane protein assembly factor BamC × 1 (W8SZY2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 32–398; UniProt 26–392

Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain P; UniProt 948–1298 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamE × 1 (A0A3L5AP29) Outer membrane protein assembly factor BamD × 1 (A0A1X3I1M6) Outer membrane protein assembly factor BamC × 1 (W8SZY2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1
Chains and sequence ranges Author chain P; PDBConstruct 403–762; UniProt 948–1298

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 22–810 Not recorded Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera × 1 (P0AEX9,Q7BSW5) Outer membrane protein assembly factor BamE × 1 (A0A3L5AP29) Outer membrane protein assembly factor BamD × 1 (A0A1X3I1M6) Outer membrane protein assembly factor BamC × 1 (W8SZY2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 2
Chains and sequence ranges Author chain A; PDBConstruct 12–800; UniProt 22–810

Outer membrane protein assembly factor BamE

Escherichia coli

UniProt A0A3L5AP29

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 20–113 Not recorded Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera × 1 (P0AEX9,Q7BSW5) Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamD × 1 (A0A1X3I1M6) Outer membrane protein assembly factor BamC × 1 (W8SZY2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A3L5AP29_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–94; UniProt 20–113

Outer membrane protein assembly factor BamD

Escherichia coli

UniProt A0A1X3I1M6

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 20–245 Not recorded Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera × 1 (P0AEX9,Q7BSW5) Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamE × 1 (A0A3L5AP29) Outer membrane protein assembly factor BamC × 1 (W8SZY2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1X3I1M6_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–226; UniProt 20–245

Outer membrane protein assembly factor BamC

Escherichia coli

UniProt W8SZY2

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 25–344 Not recorded Maltose/maltodextrin-binding periplasmic protein,Serine protease EspP chimera × 1 (P0AEX9,Q7BSW5) Outer membrane protein assembly factor BamA × 1 (C3TPJ2) Outer membrane protein assembly factor BamE × 1 (A0A3L5AP29) Outer membrane protein assembly factor BamD × 1 (A0A1X3I1M6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W8SZY2_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–320; UniProt 25–344

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 7tt5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tt5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tt5
Deposition date deposition_date2022-01-31
Structure title titleBamABCDE bound to substrate EspP in the open-sheet EspP state
Keywords keywordsmembrane protein folding, membrane dynamics, outer membrane protein, BAM, beta-barrel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.52
Radius of gyration Rg (electron density) rg_electron37.46
Forward intensity I(0) i0172023000.00
Molecular weight molecular_weight103570.0 kDa
Excluded volume excluded_volume128770 ų
Envelope volume envelope_volume203260 ų
Hydration-shell volume shell_volume47143 ų
Envelope diameter envelope_diameter132.6
Shell Rg shell_rg41.66
Envelope Rg envelope_rg37.35
Shape Rg shape_rg37.43
Total Rg total_rg37.86
Total atoms total_atoms14255
Residues n_residues928
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 dmax124.6
Rg (real space) rg_real37.63
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real1.7200e+08
I(0) uncertainty (real space) i0_real_error3.4530e+06
Rg (reciprocal space) rg_reciprocal37.57
I(0) (reciprocal space) i0_reciprocal172000000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.5
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.281
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18570000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)