9fxs

Cryo-EM structure of the type 1 pilus complex including pilus rod and FimI-bound assembly platform after incorporation of two FimI subunits - Local refinement

Method: ELECTRON MICROSCOPY Dmax: 107.9 Å Quality: GOOD

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

Fimbrin-like protein FimI

Escherichia coli

UniProt P39264

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 B; UniProt 20–179 Chain I; UniProt 20–179 Not recorded Chaperone protein FimC × 1 (P31697) Outer membrane usher protein FimD × 1 (P30130) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.20 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMI_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–160; UniProt 20–179 Author chain I; PDBConstruct 1–160; UniProt 20–179

Chaperone protein FimC

Escherichia coli

UniProt P31697

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 Fimbrin-like protein FimI × 2 (P39264) Outer membrane usher protein FimD × 1 (P30130) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.20 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 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMC_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–206; UniProt 37–241

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 Fimbrin-like protein FimI × 2 (P39264) Chaperone protein FimC × 1 (P31697) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.20 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–833; UniProt 46–878

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 9fxs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9fxs
Deposition date deposition_date2024-07-02
Structure title titleCryo-EM structure of the type 1 pilus complex including pilus rod and FimI-bound assembly platform after incorporation of two FimI subunits - Local refinement
Keywords keywordsrod, pilus, usher, termination, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.45
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i0236041000.00
Molecular weight molecular_weight120980.0 kDa
Excluded volume excluded_volume150570 ų
Envelope volume envelope_volume202680 ų
Hydration-shell volume shell_volume50698 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg40.36
Envelope Rg envelope_rg32.69
Shape Rg shape_rg32.83
Total Rg total_rg33.47
Total atoms total_atoms8535
Residues n_residues1106
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 dmax107.9
Rg (real space) rg_real33.40
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real2.3600e+08
I(0) uncertainty (real space) i0_real_error3.5900e+06
Rg (reciprocal space) rg_reciprocal33.44
I(0) (reciprocal space) i0_reciprocal236000000.0000
Solution quality estimate total_estimate0.8811
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.346
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42590000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)