9fx8

Cryo-EM structure of the FimI-bound type 1 pilus assembly platform complex - Local refinement

Method: ELECTRON MICROSCOPY Dmax: 111.7 Å Quality: GOOD

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 37–241 Not recorded Outer membrane usher protein FimD × 1 (P30130) Fimbrin-like protein FimI × 1 (P39264) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.60 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 1
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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 46–878 Not recorded Chaperone protein FimC × 1 (P31697) Fimbrin-like protein FimI × 1 (P39264) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.60 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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–833; UniProt 46–878

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count 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 3.60 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 3
Chains and sequence ranges Author chain I; PDBConstruct 1–160; UniProt 20–179

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 9fx8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fx8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fx8
Deposition date deposition_date2024-07-01
Structure title titleCryo-EM structure of the FimI-bound type 1 pilus assembly platform complex - Local refinement
Keywords keywordschaperone, usher, pilus, 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_guinier35.29
Radius of gyration Rg (electron density) rg_electron34.62
Forward intensity I(0) i0196721000.00
Molecular weight molecular_weight109670.0 kDa
Excluded volume excluded_volume136340 ų
Envelope volume envelope_volume199010 ų
Hydration-shell volume shell_volume48736 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg40.85
Envelope Rg envelope_rg33.45
Shape Rg shape_rg34.62
Total Rg total_rg35.12
Total atoms total_atoms7738
Residues n_residues1000
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 dmax111.7
Rg (real space) rg_real35.20
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.9670e+08
I(0) uncertainty (real space) i0_real_error2.5950e+06
Rg (reciprocal space) rg_reciprocal35.26
I(0) (reciprocal space) i0_reciprocal196700000.0000
Solution quality estimate total_estimate0.8789
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13310000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)