9bog

Structural basis for adhesin secretion by the outer-membrane usher in type 1 pili

Method: ELECTRON MICROSCOPY Dmax: 152.6 Å Quality: GOOD

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

Outer membrane usher protein FimD

Escherichia coli

UniProt P30130

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 46–878 Not recorded Protein FimF × 1 (P08189) Type 1 fimbria chaperone FimC × 1 (Q643I0) Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–833; UniProt 46–878

Protein FimF

Escherichia coli

UniProt P08189

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 23–176 Not recorded Outer membrane usher protein FimD × 1 (P30130) Type 1 fimbria chaperone FimC × 1 (Q643I0) Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

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

View Construct and Data Evidence
UniProt name FIMF_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–154; UniProt 23–176

Type 1 fimbria chaperone FimC

Escherichia coli

UniProt Q643I0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 37–241 Not recorded Outer membrane usher protein FimD × 1 (P30130) Protein FimF × 1 (P08189) Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q643I0_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–205; UniProt 37–241

Type 1 fimbrin D-mannose specific adhesin

Escherichia coli

UniProt P08191

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 22–300 Not recorded Outer membrane usher protein FimD × 1 (P30130) Protein FimF × 1 (P08189) Type 1 fimbria chaperone FimC × 1 (Q643I0) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

57 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMH_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–279; UniProt 22–300

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 9bog

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bog
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bog
Deposition date deposition_date2024-05-03
Structure title titleStructural basis for adhesin secretion by the outer-membrane usher in type 1 pili
Keywords keywordsOuter membrane usher, FimD, FimH, adhesin, type 1 pilus, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.93
Radius of gyration Rg (electron density) rg_electron39.33
Forward intensity I(0) i0303675000.00
Molecular weight molecular_weight132210.0 kDa
Excluded volume excluded_volume161510 ų
Envelope volume envelope_volume256490 ų
Hydration-shell volume shell_volume56356 ų
Envelope diameter envelope_diameter161.5
Shell Rg shell_rg43.41
Envelope Rg envelope_rg39.16
Shape Rg shape_rg39.42
Total Rg total_rg39.32
Total atoms total_atoms9370
Residues n_residues1438
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 dmax152.6
Rg (real space) rg_real40.25
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real3.0370e+08
I(0) uncertainty (real space) i0_real_error5.8290e+06
Rg (reciprocal space) rg_reciprocal40.05
I(0) (reciprocal space) i0_reciprocal303600000.0000
Solution quality estimate total_estimate0.7963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.603
Kurtosis Kurtosis kurtosis0.129
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40640000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.504; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.850; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)