8wlh

Cryo-EM structure of the proximal rod-export apparatus and FlgF within the motor-hook complex in the CCW state

Method: ELECTRON MICROSCOPY Dmax: 203.7 Å Quality: GOOD

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

Flagellar biosynthetic protein FliQ

OrganismNot specified

UniProt P0A1L5

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain A; UniProt 1–89 Chain B; UniProt 1–89 Chain C; UniProt 1–89 Chain D; UniProt 1–89 Not recorded Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 FLIQ_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–89; UniProt 1–89 Author chain B; PDBConstruct 1–89; UniProt 1–89 Author chain C; PDBConstruct 1–89; UniProt 1–89 Author chain D; PDBConstruct 1–89; UniProt 1–89

Flagellar biosynthetic protein FliR

OrganismNot specified

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain E; UniProt 1–264 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 E; PDBConstruct 1–264; UniProt 1–264

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain F; UniProt 1–245 Chain G; UniProt 1–245 Chain H; UniProt 1–245 Chain I; UniProt 1–245 Chain J; UniProt 1–245 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–245; UniProt 1–245 Author chain G; PDBConstruct 1–245; UniProt 1–245 Author chain H; PDBConstruct 1–245; UniProt 1–245 Author chain I; PDBConstruct 1–245; UniProt 1–245 Author chain J; PDBConstruct 1–245; UniProt 1–245

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain K; UniProt 1–104 Chain L; UniProt 1–104 Chain M; UniProt 1–104 Chain N; UniProt 1–104 Chain O; UniProt 1–104 Chain P; UniProt 1–104 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 4
Chains and sequence ranges Author chain K; PDBConstruct 1–104; UniProt 1–104 Author chain L; PDBConstruct 1–104; UniProt 1–104 Author chain M; PDBConstruct 1–104; UniProt 1–104 Author chain N; PDBConstruct 1–104; UniProt 1–104 Author chain O; PDBConstruct 1–104; UniProt 1–104 Author chain P; PDBConstruct 1–104; UniProt 1–104

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain Q; UniProt 1–138 Chain R; UniProt 1–138 Chain S; UniProt 1–138 Chain T; UniProt 1–138 Chain U; UniProt 1–138 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–138; UniProt 1–138 Author chain R; PDBConstruct 1–138; UniProt 1–138 Author chain S; PDBConstruct 1–138; UniProt 1–138 Author chain T; PDBConstruct 1–138; UniProt 1–138 Author chain U; PDBConstruct 1–138; UniProt 1–138

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain V; UniProt 1–134 Chain W; UniProt 1–134 Chain X; UniProt 1–134 Chain Y; UniProt 1–134 Chain Z; UniProt 1–134 Chain a; UniProt 1–134 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 6
Chains and sequence ranges Author chain V; PDBConstruct 1–134; UniProt 1–134 Author chain W; PDBConstruct 1–134; UniProt 1–134 Author chain X; PDBConstruct 1–134; UniProt 1–134 Author chain Y; PDBConstruct 1–134; UniProt 1–134 Author chain Z; PDBConstruct 1–134; UniProt 1–134 Author chain a; PDBConstruct 1–134; UniProt 1–134

Flagellar M-ring protein

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain b; UniProt 1–560 Chain c; UniProt 1–560 Chain d; UniProt 1–560 Chain e; UniProt 1–560 Chain f; UniProt 1–560 Chain g; UniProt 1–560 Chain h; UniProt 1–560 Chain i; UniProt 1–560 Chain j; UniProt 1–560 Chain k; UniProt 1–560 Chain l; UniProt 1–560 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal-body rod protein FlgF × 5 (P16323) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 7
Chains and sequence ranges Author chain b; PDBConstruct 1–560; UniProt 1–560 Author chain c; PDBConstruct 1–560; UniProt 1–560 Author chain d; PDBConstruct 1–560; UniProt 1–560 Author chain e; PDBConstruct 1–560; UniProt 1–560 Author chain f; PDBConstruct 1–560; UniProt 1–560 Author chain g; PDBConstruct 1–560; UniProt 1–560 Author chain h; PDBConstruct 1–560; UniProt 1–560 Author chain i; PDBConstruct 1–560; UniProt 1–560 Author chain j; PDBConstruct 1–560; UniProt 1–560 Author chain k; PDBConstruct 1–560; UniProt 1–560 Author chain l; PDBConstruct 1–560; UniProt 1–560

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 × 43 PDB declaration: 43-meric(43) Consistent with protein copy count Chain m; UniProt 1–251 Chain n; UniProt 1–251 Chain o; UniProt 1–251 Chain p; UniProt 1–251 Chain q; UniProt 1–251 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 2 Blot force: -15 Wait time: 60 Blot total: 1 Resolution 3.70 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 8
Chains and sequence ranges Author chain m; PDBConstruct 1–251; UniProt 1–251 Author chain n; PDBConstruct 1–251; UniProt 1–251 Author chain o; PDBConstruct 1–251; UniProt 1–251 Author chain p; PDBConstruct 1–251; UniProt 1–251 Author chain q; PDBConstruct 1–251; UniProt 1–251

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 8wlh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wlh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wlh
Deposition date deposition_date2023-09-29
Structure title titleCryo-EM structure of the proximal rod-export apparatus and FlgF within the motor-hook complex in the CCW state
Keywords keywordsFlagellum, Flagellar motor, Proximal rod, Export apparatus, FlgF, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.69
Radius of gyration Rg (electron density) rg_electron64.27
Forward intensity I(0) i03600400000.00
Molecular weight molecular_weight516830.0 kDa
Excluded volume excluded_volume652770 ų
Envelope volume envelope_volume936040 ų
Hydration-shell volume shell_volume125990 ų
Envelope diameter envelope_diameter245.1
Shell Rg shell_rg60.19
Envelope Rg envelope_rg64.21
Shape Rg shape_rg64.28
Total Rg total_rg64.12
Total atoms total_atoms36230
Residues n_residues4845
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 dmax203.7
Rg (real space) rg_real63.09
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real3.5950e+09
I(0) uncertainty (real space) i0_real_error7.1930e+07
Rg (reciprocal space) rg_reciprocal62.12
I(0) (reciprocal space) i0_reciprocal3593000000.0000
Solution quality estimate total_estimate0.8143
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.2
Skewness Skewness skewness0.599
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0079
Highest regularization parameter α highest_alpha491500000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.212

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)