6r69

Improved map of the FliPQR complex that forms the core of the Salmonella type III secretion system export apparatus.

Method: ELECTRON MICROSCOPY Dmax: 112.2 Å Quality: GOOD

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

Flagellar biosynthetic protein FliP

Salmonella enterica subsp. enterica

UniProt G5QE81

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–245 Chain B; UniProt 1–245 Chain C; UniProt 1–245 Chain D; UniProt 1–245 Chain E; UniProt 1–245 Not recorded Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliQ × 4 (A0A0M0QTK6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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 G5QE81_SALRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–245; UniProt 1–245 Author chain B; PDBConstruct 1–245; UniProt 1–245 Author chain C; PDBConstruct 1–245; UniProt 1–245 Author chain D; PDBConstruct 1–245; UniProt 1–245 Author chain E; PDBConstruct 1–245; UniProt 1–245

Flagellar biosynthetic protein FliR

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P54702

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain F; UniProt 1–264 Not recorded Flagellar biosynthetic protein FliP × 5 (G5QE81) Flagellar biosynthetic protein FliQ × 4 (A0A0M0QTK6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIR_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–264; UniProt 1–264

Flagellar biosynthetic protein FliQ

Salmonella enterica

UniProt A0A0M0QTK6

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–89 Chain H; UniProt 1–89 Chain I; UniProt 1–89 Chain J; UniProt 1–89 Not recorded Flagellar biosynthetic protein FliP × 5 (G5QE81) Flagellar biosynthetic protein FliR × 1 (P54702) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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 A0A0M0QTK6_SALER
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–89; UniProt 1–89 Author chain H; PDBConstruct 1–89; UniProt 1–89 Author chain I; PDBConstruct 1–89; UniProt 1–89 Author chain J; PDBConstruct 1–89; UniProt 1–89

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 6r69

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6r69
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6r69
Deposition date deposition_date2019-03-26
Structure title titleImproved map of the FliPQR complex that forms the core of the Salmonella type III secretion system export apparatus.
Keywords keywordsT3SS, Flagella, Cryo-EM, Export, Membrane protein, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.53
Radius of gyration Rg (electron density) rg_electron35.01
Forward intensity I(0) i0370623000.00
Molecular weight molecular_weight178440.0 kDa
Excluded volume excluded_volume233420 ų
Envelope volume envelope_volume311460 ų
Hydration-shell volume shell_volume69792 ų
Envelope diameter envelope_diameter123.1
Shell Rg shell_rg44.47
Envelope Rg envelope_rg34.54
Shape Rg shape_rg35.01
Total Rg total_rg35.78
Total atoms total_atoms12541
Residues n_residues1629
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 dmax112.2
Rg (real space) rg_real36.23
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.7060e+08
I(0) uncertainty (real space) i0_real_error5.2570e+06
Rg (reciprocal space) rg_reciprocal36.42
I(0) (reciprocal space) i0_reciprocal370700000.0000
Solution quality estimate total_estimate0.8923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.6
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha226200000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)