6e14

Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD

Method: ELECTRON MICROSCOPY Dmax: 184.0 Å Quality: REASONABLE

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

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 1–300 Not recorded Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 1
Chains and sequence ranges Author chain H; PDBConstruct 1–300; UniProt 1–300

Fimbrial biogenesis outer membrane usher protein

Escherichia coli

UniProt A0A0F3W955

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–878 Not recorded Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 A0A0F3W955_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–878; UniProt 1–878

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 22–176 Not recorded Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimG × 1 (P08190) Chaperone protein FimC × 1 (P31697) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 3
Chains and sequence ranges Author chain F; PDBConstruct 2–156; UniProt 22–176

Protein FimG

Escherichia coli

UniProt P08190

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 11–167 Not recorded Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Chaperone protein FimC × 1 (P31697) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

15 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMG_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 2–158; UniProt 11–167

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–241 Not recorded Type 1 fimbrin D-mannose specific adhesin × 1 (P08191) Fimbrial biogenesis outer membrane usher protein × 1 (A0A0F3W955) Protein FimF × 1 (P08189) Protein FimG × 1 (P08190) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 5
Chains and sequence ranges Author chain C; PDBConstruct 1–241; UniProt 1–241

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 6e14

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e14
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e14
Deposition date deposition_date2018-07-09
Structure title titleHandover mechanism of the growing pilus by the bacterial outer membrane usher FimD
Keywords keywordspili, chaperone, usher, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.83
Radius of gyration Rg (electron density) rg_electron48.26
Forward intensity I(0) i0455143000.00
Molecular weight molecular_weight170110.0 kDa
Excluded volume excluded_volume211230 ų
Envelope volume envelope_volume332390 ų
Hydration-shell volume shell_volume65217 ų
Envelope diameter envelope_diameter193.9
Shell Rg shell_rg45.59
Envelope Rg envelope_rg48.20
Shape Rg shape_rg48.25
Total Rg total_rg48.16
Total atoms total_atoms11991
Residues n_residues1586
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 dmax184.0
Rg (real space) rg_real47.93
Rg uncertainty (real space) rg_real_error2.40
I(0) (real space) i0_real4.5510e+08
I(0) uncertainty (real space) i0_real_error9.4170e+06
Rg (reciprocal space) rg_reciprocal46.83
I(0) (reciprocal space) i0_reciprocal454500000.0000
Solution quality estimate total_estimate0.7280
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.3
Skewness Skewness skewness0.942
Kurtosis Kurtosis kurtosis0.670
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76530000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.308; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.759; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6e14C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6e14G00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id6e14H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id6e14H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain

8. Citations (1)

9. Files and Curves (10)