7cg4

Cryo-EM structure of the flagellar export apparatus with FliE from Salmonella

Method: ELECTRON MICROSCOPY Dmax: 118.5 Å Quality: REASONABLE

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

Flagellar hook-basal body complex protein FliE

OrganismNot specified

UniProt P26462

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain a; UniProt 1–104 Chain b; UniProt 1–104 Chain c; UniProt 1–104 Chain d; UniProt 1–104 Chain e; UniProt 1–104 Chain f; UniProt 1–104 Not recorded Flagellar biosynthetic protein FliP × 5 (P54700) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging 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.

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

View Construct and Data Evidence
UniProt name FLIE_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–104; UniProt 1–104 Author chain b; PDBConstruct 1–104; UniProt 1–104 Author chain c; PDBConstruct 1–104; UniProt 1–104 Author chain d; PDBConstruct 1–104; UniProt 1–104 Author chain e; PDBConstruct 1–104; UniProt 1–104 Author chain f; PDBConstruct 1–104; UniProt 1–104

Flagellar biosynthetic protein FliP

OrganismNot specified

UniProt P54700

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain r; UniProt 1–245 Chain s; UniProt 1–245 Chain t; UniProt 1–245 Chain u; UniProt 1–245 Chain v; UniProt 1–245 Not recorded Flagellar hook-basal body complex protein FliE × 6 (P26462) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging 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 FLIP_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain r; PDBConstruct 1–245; UniProt 1–245 Author chain s; PDBConstruct 1–245; UniProt 1–245 Author chain t; PDBConstruct 1–245; UniProt 1–245 Author chain u; PDBConstruct 1–245; UniProt 1–245 Author chain v; PDBConstruct 1–245; UniProt 1–245

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 7cg4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7cg4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7cg4
Deposition date deposition_date2020-06-30
Structure title titleCryo-EM structure of the flagellar export apparatus with FliE from Salmonella
Keywords keywordsExport apparatus, FliE, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.82
Radius of gyration Rg (electron density) rg_electron36.58
Forward intensity I(0) i0321042000.00
Molecular weight molecular_weight156040.0 kDa
Excluded volume excluded_volume200600 ų
Envelope volume envelope_volume294700 ų
Hydration-shell volume shell_volume64759 ų
Envelope diameter envelope_diameter127.7
Shell Rg shell_rg44.89
Envelope Rg envelope_rg35.66
Shape Rg shape_rg36.58
Total Rg total_rg37.24
Total atoms total_atoms10943
Residues n_residues1419
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 dmax118.5
Rg (real space) rg_real37.53
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real3.2100e+08
I(0) uncertainty (real space) i0_real_error5.1570e+06
Rg (reciprocal space) rg_reciprocal37.71
I(0) (reciprocal space) i0_reciprocal321100000.0000
Solution quality estimate total_estimate0.6750
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.8
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74670000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 0.080; Positv: 1.000; Valcen: 0.957; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)