7nsu

ColicinE9 intact translocation complex

Method: ELECTRON MICROSCOPY Dmax: 169.8 Å Quality: GOOD

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

Outer membrane protein F

Escherichia coli (strain K12)

UniProt P02931

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 23–362 Chain B; UniProt 23–362 Chain C; UniProt 23–362 Not recorded Colicin-E9 × 1 (P09883) Tol-Pal system protein TolB × 1 (A0A6D2XIU5) Vitamin B12 transporter BtuB × 1 (P06129) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of diluted translocon preparation were applied on freshly glow discharged grids coated with graphene oxide (as described in https://doi.org/10.1038/s41594-019-0355-2); after 30sec waiting grids were blotted for 8-10 using -10 force and plunge frozen in liquid ethane Resolution 4.70 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.

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

View Construct and Data Evidence
UniProt name OMPF_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 23–362 Author chain B; PDBConstruct 1–340; UniProt 23–362 Author chain C; PDBConstruct 1–340; UniProt 23–362

Colicin-E9

Escherichia coli

UniProt P09883

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 1–582 Mutation:A33C Outer membrane protein F × 3 (P02931) Tol-Pal system protein TolB × 1 (A0A6D2XIU5) Vitamin B12 transporter BtuB × 1 (P06129) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of diluted translocon preparation were applied on freshly glow discharged grids coated with graphene oxide (as described in https://doi.org/10.1038/s41594-019-0355-2); after 30sec waiting grids were blotted for 8-10 using -10 force and plunge frozen in liquid ethane Resolution 4.70 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.

24 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEA9_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–582; UniProt 1–582

Tol-Pal system protein TolB

Escherichia coli (strain K12)

UniProt A0A6D2XIU5

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 1–430 Mutation:P201C Outer membrane protein F × 3 (P02931) Colicin-E9 × 1 (P09883) Vitamin B12 transporter BtuB × 1 (P06129) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of diluted translocon preparation were applied on freshly glow discharged grids coated with graphene oxide (as described in https://doi.org/10.1038/s41594-019-0355-2); after 30sec waiting grids were blotted for 8-10 using -10 force and plunge frozen in liquid ethane Resolution 4.70 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 A0A6D2XIU5_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–430; UniProt 1–430

Vitamin B12 transporter BtuB

Escherichia coli (strain K12)

UniProt P06129

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 F; UniProt 21–614 Not recorded Outer membrane protein F × 3 (P02931) Colicin-E9 × 1 (P09883) Tol-Pal system protein TolB × 1 (A0A6D2XIU5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of diluted translocon preparation were applied on freshly glow discharged grids coated with graphene oxide (as described in https://doi.org/10.1038/s41594-019-0355-2); after 30sec waiting grids were blotted for 8-10 using -10 force and plunge frozen in liquid ethane Resolution 4.70 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BTUB_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–594; UniProt 21–614

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 7nsu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7nsu
Deposition date deposition_date2021-03-08
Structure title titleColicinE9 intact translocation complex
Keywords keywordsbacteriocin complex, import, membrane, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.12
Radius of gyration Rg (electron density) rg_electron49.24
Forward intensity I(0) i01065210000.00
Molecular weight molecular_weight261250.0 kDa
Excluded volume excluded_volume322700 ų
Envelope volume envelope_volume482670 ų
Hydration-shell volume shell_volume84122 ų
Envelope diameter envelope_diameter180.1
Shell Rg shell_rg51.24
Envelope Rg envelope_rg48.06
Shape Rg shape_rg49.21
Total Rg total_rg49.42
Total atoms total_atoms35926
Residues n_residues2410
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 dmax169.8
Rg (real space) rg_real49.10
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real1.0650e+09
I(0) uncertainty (real space) i0_real_error1.9410e+07
Rg (reciprocal space) rg_reciprocal49.12
I(0) (reciprocal space) i0_reciprocal1065000000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.4
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.257
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80490000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)