9fx0

Cryo-EM structure of the type 1 pilus tip-to-rod transition

Method: ELECTRON MICROSCOPY Dmax: 98.2 Å Quality: GOOD

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

Type-1 fimbrial protein, A chain

Escherichia coli

UniProt P04128

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 24–182 Chain B; UniProt 24–182 Chain C; UniProt 24–182 Chain D; UniProt 24–182 Chain E; UniProt 24–182 Chain G; UniProt 24–182 Not recorded Protein FimF × 1 (P08189) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMA1_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–160; UniProt 24–182 Author chain B; PDBConstruct 2–160; UniProt 24–182 Author chain C; PDBConstruct 2–160; UniProt 24–182 Author chain D; PDBConstruct 2–160; UniProt 24–182 Author chain E; PDBConstruct 2–160; UniProt 24–182 Author chain G; PDBConstruct 2–160; UniProt 24–182

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 23–176 Not recorded Type-1 fimbrial protein, A chain × 6 (P04128) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.10 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

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 9fx0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fx0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fx0
Deposition date deposition_date2024-07-01
Structure title titleCryo-EM structure of the type 1 pilus tip-to-rod transition
Keywords keywordsrod, tip, usher, pilus, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.16
Radius of gyration Rg (electron density) rg_electron31.19
Forward intensity I(0) i0207204000.00
Molecular weight molecular_weight109070.0 kDa
Excluded volume excluded_volume134250 ų
Envelope volume envelope_volume177200 ų
Hydration-shell volume shell_volume46463 ų
Envelope diameter envelope_diameter104.1
Shell Rg shell_rg39.04
Envelope Rg envelope_rg30.58
Shape Rg shape_rg31.17
Total Rg total_rg31.90
Total atoms total_atoms7673
Residues n_residues1088
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 dmax98.2
Rg (real space) rg_real31.96
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real2.0720e+08
I(0) uncertainty (real space) i0_real_error2.7520e+06
Rg (reciprocal space) rg_reciprocal32.05
I(0) (reciprocal space) i0_reciprocal207200000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.158
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45120000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)