7e82

Cryo-EM structure of the flagellar rod with partial hook from Salmonella

Method: ELECTRON MICROSCOPY Dmax: 248.8 Å Quality: EXCELLENT

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

Flagellar basal-body rod protein FlgG

OrganismNot specified

UniProt P0A1J3

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain A; UniProt 1–260 Chain B; UniProt 1–260 Chain C; UniProt 1–260 Chain D; UniProt 1–260 Chain E; UniProt 1–260 Chain F; UniProt 1–260 Chain G; UniProt 1–260 Chain H; UniProt 1–260 Chain I; UniProt 1–260 Chain J; UniProt 1–260 Chain K; UniProt 1–260 Chain L; UniProt 1–260 Chain M; UniProt 1–260 Chain N; UniProt 1–260 Chain O; UniProt 1–260 Chain P; UniProt 1–260 Chain Q; UniProt 1–260 Chain R; UniProt 1–260 Chain S; UniProt 1–260 Chain T; UniProt 1–260 Chain U; UniProt 1–260 Chain V; UniProt 1–260 Chain W; UniProt 1–260 Chain X; UniProt 1–260 Not recorded Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGG_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–260; UniProt 1–260 Author chain B; PDBConstruct 1–260; UniProt 1–260 Author chain C; PDBConstruct 1–260; UniProt 1–260 Author chain D; PDBConstruct 1–260; UniProt 1–260 Author chain E; PDBConstruct 1–260; UniProt 1–260 Author chain F; PDBConstruct 1–260; UniProt 1–260 Author chain G; PDBConstruct 1–260; UniProt 1–260 Author chain H; PDBConstruct 1–260; UniProt 1–260 Author chain I; PDBConstruct 1–260; UniProt 1–260 Author chain J; PDBConstruct 1–260; UniProt 1–260 Author chain K; PDBConstruct 1–260; UniProt 1–260 Author chain L; PDBConstruct 1–260; UniProt 1–260 Author chain M; PDBConstruct 1–260; UniProt 1–260 Author chain N; PDBConstruct 1–260; UniProt 1–260 Author chain O; PDBConstruct 1–260; UniProt 1–260 Author chain P; PDBConstruct 1–260; UniProt 1–260 Author chain Q; PDBConstruct 1–260; UniProt 1–260 Author chain R; PDBConstruct 1–260; UniProt 1–260 Author chain S; PDBConstruct 1–260; UniProt 1–260 Author chain T; PDBConstruct 1–260; UniProt 1–260 Author chain U; PDBConstruct 1–260; UniProt 1–260 Author chain V; PDBConstruct 1–260; UniProt 1–260 Author chain W; PDBConstruct 1–260; UniProt 1–260 Author chain X; PDBConstruct 1–260; UniProt 1–260

Flagellar basal-body rod protein FlgF

OrganismNot specified

UniProt P16323

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain a; UniProt 1–251 Chain b; UniProt 1–251 Chain c; UniProt 1–251 Chain d; UniProt 1–251 Chain e; UniProt 1–251 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGF_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–251; UniProt 1–251 Author chain b; PDBConstruct 1–251; UniProt 1–251 Author chain c; PDBConstruct 1–251; UniProt 1–251 Author chain d; PDBConstruct 1–251; UniProt 1–251 Author chain e; PDBConstruct 1–251; UniProt 1–251

Flagellar MS ring L1

OrganismNot specified

UniProt P15928

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain 5; UniProt 311–331 Chain 6; UniProt 311–331 Chain 7; UniProt 311–331 Chain 8; UniProt 311–331 Chain 9; UniProt 311–331 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIF_SALTY
Isoform
PDB entities 4
Chains and sequence ranges Author chain 5; PDBConstruct 1–21; UniProt 311–331 Author chain 6; PDBConstruct 1–21; UniProt 311–331 Author chain 7; PDBConstruct 1–21; UniProt 311–331 Author chain 8; PDBConstruct 1–21; UniProt 311–331 Author chain 9; PDBConstruct 1–21; UniProt 311–331

Flagellar basal-body rod protein FlgC

OrganismNot specified

UniProt P0A1I7

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain f; UniProt 1–134 Chain g; UniProt 1–134 Chain h; UniProt 1–134 Chain i; UniProt 1–134 Chain j; UniProt 1–134 Chain p; UniProt 1–134 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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 FLGC_SALTY
Isoform
PDB entities 5
Chains and sequence ranges Author chain f; PDBConstruct 1–134; UniProt 1–134 Author chain g; PDBConstruct 1–134; UniProt 1–134 Author chain h; PDBConstruct 1–134; UniProt 1–134 Author chain i; PDBConstruct 1–134; UniProt 1–134 Author chain j; PDBConstruct 1–134; UniProt 1–134 Author chain p; PDBConstruct 1–134; UniProt 1–134

Flagellar basal body rod protein FlgB

OrganismNot specified

UniProt P16437

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain k; UniProt 1–138 Chain l; UniProt 1–138 Chain m; UniProt 1–138 Chain n; UniProt 1–138 Chain o; UniProt 1–138 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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 FLGB_SALTY
Isoform
PDB entities 6
Chains and sequence ranges Author chain k; PDBConstruct 1–138; UniProt 1–138 Author chain l; PDBConstruct 1–138; UniProt 1–138 Author chain m; PDBConstruct 1–138; UniProt 1–138 Author chain n; PDBConstruct 1–138; UniProt 1–138 Author chain o; PDBConstruct 1–138; UniProt 1–138

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain q; UniProt 1–104 Chain r; UniProt 1–104 Chain s; UniProt 1–104 Chain t; UniProt 1–104 Chain u; UniProt 1–104 Chain v; UniProt 1–104 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar hook protein FlgE × 11 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds before plunging Resolution 3.30 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 7
Chains and sequence ranges Author chain q; PDBConstruct 1–104; UniProt 1–104 Author chain r; PDBConstruct 1–104; UniProt 1–104 Author chain s; PDBConstruct 1–104; UniProt 1–104 Author chain t; PDBConstruct 1–104; UniProt 1–104 Author chain u; PDBConstruct 1–104; UniProt 1–104 Author chain v; PDBConstruct 1–104; UniProt 1–104

Flagellar hook protein FlgE

OrganismNot specified

UniProt P0A1J1

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 × 67 PDB declaration: 67-meric(67) Consistent with protein copy count Chain DA; UniProt 1–403 Chain DB; UniProt 1–403 Chain DC; UniProt 1–403 Chain DD; UniProt 1–403 Chain DE; UniProt 1–403 Chain DF; UniProt 1–403 Chain DG; UniProt 1–403 Chain DH; UniProt 1–403 Chain DI; UniProt 1–403 Chain DJ; UniProt 1–403 Chain DK; UniProt 1–403 Not recorded Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar MS ring L2 × 5 Flagellar MS ring L1 × 5 (P15928) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal body rod protein FlgB × 5 (P16437) 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 3.30 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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGE_SALTY
Isoform
PDB entities 8
Chains and sequence ranges Author chain DA; PDBConstruct 1–403; UniProt 1–403 Author chain DB; PDBConstruct 1–403; UniProt 1–403 Author chain DC; PDBConstruct 1–403; UniProt 1–403 Author chain DD; PDBConstruct 1–403; UniProt 1–403 Author chain DE; PDBConstruct 1–403; UniProt 1–403 Author chain DF; PDBConstruct 1–403; UniProt 1–403 Author chain DG; PDBConstruct 1–403; UniProt 1–403 Author chain DH; PDBConstruct 1–403; UniProt 1–403 Author chain DI; PDBConstruct 1–403; UniProt 1–403 Author chain DJ; PDBConstruct 1–403; UniProt 1–403 Author chain DK; PDBConstruct 1–403; UniProt 1–403

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 7e82

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7e82
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7e82
Deposition date deposition_date2021-02-28
Structure title titleCryo-EM structure of the flagellar rod with partial hook from Salmonella
Keywords keywordsFlagella, Rod, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier88.75
Radius of gyration Rg (electron density) rg_electron89.80
Forward intensity I(0) i031192800000.00
Molecular weight molecular_weight1446700.0 kDa
Excluded volume excluded_volume1788100 ų
Envelope volume envelope_volume2702200 ų
Hydration-shell volume shell_volume256660 ų
Envelope diameter envelope_diameter361.6
Shell Rg shell_rg83.78
Envelope Rg envelope_rg92.72
Shape Rg shape_rg89.76
Total Rg total_rg89.88
Total atoms total_atoms101606
Residues n_residues13700
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 dmax248.8
Rg (real space) rg_real82.94
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.9760e+10
I(0) uncertainty (real space) i0_real_error5.8270e+08
Rg (reciprocal space) rg_reciprocal85.14
I(0) (reciprocal space) i0_reciprocal30860000000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary82.9
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.5477
Highest regularization parameter α highest_alpha3338000000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.952; Stabil: 0.984; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.021

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)