7nri

Structure of the darobactin-bound E. coli BAM complex (BamABCDE)

Method: ELECTRON MICROSCOPY Dmax: 134.7 Å Quality: GOOD

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

Outer membrane protein assembly factor BamA

Escherichia coli (strain K12)

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 21–808 Not recorded 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) 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4microL of sample applied Resolution 3.03 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 1–788; UniProt 21–808

Outer membrane protein assembly factor BamB

Escherichia coli (strain K12)

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 20–392 Not recorded 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) 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4microL of sample applied Resolution 3.03 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 (strain K12)

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 Protein heterocomplex 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) 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4microL of sample applied Resolution 3.03 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 (strain K12)

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 Protein heterocomplex 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) 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4microL of sample applied Resolution 3.03 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 (strain K12)

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 Protein heterocomplex 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) 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4microL of sample applied Resolution 3.03 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

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 7nri

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nri
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7nri
Deposition date deposition_date2021-03-03
Structure title titleStructure of the darobactin-bound E. coli BAM complex (BamABCDE)
Keywords keywords;Beta-Barrel, outer membrane, protein insertion, protein folding, protein maturation, antibiotic, natural product, cyclized peptide, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.42
Radius of gyration Rg (electron density) rg_electron42.92
Forward intensity I(0) i0428451000.00
Molecular weight molecular_weight167000.0 kDa
Excluded volume excluded_volume207730 ų
Envelope volume envelope_volume308580 ų
Hydration-shell volume shell_volume60715 ų
Envelope diameter envelope_diameter143.8
Shell Rg shell_rg47.96
Envelope Rg envelope_rg41.21
Shape Rg shape_rg42.92
Total Rg total_rg43.18
Total atoms total_atoms23151
Residues n_residues1504
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 dmax134.7
Rg (real space) rg_real43.21
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real4.2850e+08
I(0) uncertainty (real space) i0_real_error6.8050e+06
Rg (reciprocal space) rg_reciprocal43.42
I(0) (reciprocal space) i0_reciprocal428600000.0000
Solution quality estimate total_estimate0.8955
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.3
Skewness Skewness skewness0.013
Kurtosis Kurtosis kurtosis-0.658
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47490000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7nriA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id7nriA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id7nriA03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id7nriA04
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id7nriA05
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily310 — membrane protein fhac
Domain ID domain_id7nriA06
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology160 — Porin
Homologous superfamily homologous superfamily50 — membrane protein fhac: a member of the omp85/tpsb transporter family

8. Citations (1)

9. Files and Curves (10)