8wkq

Cryo-EM structure of the MS ring (C1) with export apparatus and proximal rod within the flagellar motor-hook complex in the CW state.

Method: ELECTRON MICROSCOPY Dmax: 279.3 Å Quality: EXCELLENT

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

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 × 103 PDB declaration: 103-meric(103) Consistent with protein copy count Chain 0; UniProt 1–560 Chain 1; UniProt 1–560 Chain 2; UniProt 1–560 Chain 3; UniProt 1–560 Chain 4; UniProt 1–560 Chain 5; UniProt 1–560 Chain 6; UniProt 1–560 Chain 7; UniProt 1–560 Chain 8; UniProt 1–560 Chain 9; UniProt 1–560 Chain AA; UniProt 1–560 Chain AB; UniProt 1–560 Chain AC; UniProt 1–560 Chain AD; UniProt 1–560 Chain AE; UniProt 1–560 Chain AF; UniProt 1–560 Chain AG; UniProt 1–560 Chain AH; UniProt 1–560 Chain AI; UniProt 1–560 Chain AJ; UniProt 1–560 Chain AK; UniProt 1–560 Chain AL; UniProt 1–560 Chain AM; UniProt 1–560 Chain AN; UniProt 1–560 Chain AO; UniProt 1–560 Chain AP; UniProt 1–560 Chain AQ; UniProt 1–560 Chain UI; UniProt 1–560 Chain UJ; UniProt 1–560 Chain UK; UniProt 1–560 Chain UL; UniProt 1–560 Chain UM; UniProt 1–560 Chain UN; UniProt 1–560 Chain UO; UniProt 1–560 Chain UP; UniProt 1–560 Chain WA; UniProt 1–560 Chain WB; UniProt 1–560 Chain WC; UniProt 1–560 Chain WD; UniProt 1–560 Chain WE; UniProt 1–560 Chain WF; UniProt 1–560 Chain WG; UniProt 1–560 Chain WH; UniProt 1–560 Chain WI; UniProt 1–560 Chain WJ; UniProt 1–560 Chain WK; UniProt 1–560 Chain WL; UniProt 1–560 Chain WM; UniProt 1–560 Chain WN; UniProt 1–560 Chain WO; UniProt 1–560 Chain WP; UniProt 1–560 Chain WQ; UniProt 1–560 Chain WR; UniProt 1–560 Chain WS; UniProt 1–560 Chain WT; UniProt 1–560 Chain WU; UniProt 1–560 Chain WV; UniProt 1–560 Chain WW; UniProt 1–560 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 Chain t; UniProt 1–560 Chain u; UniProt 1–560 Chain v; UniProt 1–560 Chain w; UniProt 1–560 Chain x; UniProt 1–560 Chain y; UniProt 1–560 Chain z; 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–560; UniProt 1–560 Author chain 1; PDBConstruct 1–560; UniProt 1–560 Author chain 2; PDBConstruct 1–560; UniProt 1–560 Author chain 3; PDBConstruct 1–560; UniProt 1–560 Author chain 4; PDBConstruct 1–560; UniProt 1–560 Author chain 5; PDBConstruct 1–560; UniProt 1–560 Author chain 6; PDBConstruct 1–560; UniProt 1–560 Author chain 7; PDBConstruct 1–560; UniProt 1–560 Author chain 8; PDBConstruct 1–560; UniProt 1–560 Author chain 9; PDBConstruct 1–560; UniProt 1–560 Author chain AA; PDBConstruct 1–560; UniProt 1–560 Author chain AB; PDBConstruct 1–560; UniProt 1–560 Author chain AC; PDBConstruct 1–560; UniProt 1–560 Author chain AD; PDBConstruct 1–560; UniProt 1–560 Author chain AE; PDBConstruct 1–560; UniProt 1–560 Author chain AF; PDBConstruct 1–560; UniProt 1–560 Author chain AG; PDBConstruct 1–560; UniProt 1–560 Author chain AH; PDBConstruct 1–560; UniProt 1–560 Author chain AI; PDBConstruct 1–560; UniProt 1–560 Author chain AJ; PDBConstruct 1–560; UniProt 1–560 Author chain AK; PDBConstruct 1–560; UniProt 1–560 Author chain AL; PDBConstruct 1–560; UniProt 1–560 Author chain AM; PDBConstruct 1–560; UniProt 1–560 Author chain AN; PDBConstruct 1–560; UniProt 1–560 Author chain AO; PDBConstruct 1–560; UniProt 1–560 Author chain AP; PDBConstruct 1–560; UniProt 1–560 Author chain AQ; PDBConstruct 1–560; UniProt 1–560 Author chain UI; PDBConstruct 1–560; UniProt 1–560 Author chain UJ; PDBConstruct 1–560; UniProt 1–560 Author chain UK; PDBConstruct 1–560; UniProt 1–560 Author chain UL; PDBConstruct 1–560; UniProt 1–560 Author chain UM; PDBConstruct 1–560; UniProt 1–560 Author chain UN; PDBConstruct 1–560; UniProt 1–560 Author chain UO; PDBConstruct 1–560; UniProt 1–560 Author chain UP; PDBConstruct 1–560; UniProt 1–560 Author chain WA; PDBConstruct 1–560; UniProt 1–560 Author chain WB; PDBConstruct 1–560; UniProt 1–560 Author chain WC; PDBConstruct 1–560; UniProt 1–560 Author chain WD; PDBConstruct 1–560; UniProt 1–560 Author chain WE; PDBConstruct 1–560; UniProt 1–560 Author chain WF; PDBConstruct 1–560; UniProt 1–560 Author chain WG; PDBConstruct 1–560; UniProt 1–560 Author chain WH; PDBConstruct 1–560; UniProt 1–560 Author chain WI; PDBConstruct 1–560; UniProt 1–560 Author chain WJ; PDBConstruct 1–560; UniProt 1–560 Author chain WK; PDBConstruct 1–560; UniProt 1–560 Author chain WL; PDBConstruct 1–560; UniProt 1–560 Author chain WM; PDBConstruct 1–560; UniProt 1–560 Author chain WN; PDBConstruct 1–560; UniProt 1–560 Author chain WO; PDBConstruct 1–560; UniProt 1–560 Author chain WP; PDBConstruct 1–560; UniProt 1–560 Author chain WQ; PDBConstruct 1–560; UniProt 1–560 Author chain WR; PDBConstruct 1–560; UniProt 1–560 Author chain WS; PDBConstruct 1–560; UniProt 1–560 Author chain WT; PDBConstruct 1–560; UniProt 1–560 Author chain WU; PDBConstruct 1–560; UniProt 1–560 Author chain WV; PDBConstruct 1–560; UniProt 1–560 Author chain WW; PDBConstruct 1–560; UniProt 1–560 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 Author chain t; PDBConstruct 1–560; UniProt 1–560 Author chain u; PDBConstruct 1–560; UniProt 1–560 Author chain v; PDBConstruct 1–560; UniProt 1–560 Author chain w; PDBConstruct 1–560; UniProt 1–560 Author chain x; PDBConstruct 1–560; UniProt 1–560 Author chain y; PDBConstruct 1–560; UniProt 1–560 Author chain z; PDBConstruct 1–560; UniProt 1–560

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 × 103 PDB declaration: 103-meric(103) 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 M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 2
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 × 103 PDB declaration: 103-meric(103) Consistent with protein copy count Chain E; UniProt 1–264 Not recorded Flagellar M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 3
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 × 103 PDB declaration: 103-meric(103) 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 M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 4
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 × 103 PDB declaration: 103-meric(103) 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 M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 5
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 × 103 PDB declaration: 103-meric(103) 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 M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 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 × 103 PDB declaration: 103-meric(103) 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 M-ring protein × 76 (P15928) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.80 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 7
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

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 8wkq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wkq
Deposition date deposition_date2023-09-28
Structure title titleCryo-EM structure of the MS ring (C1) with export apparatus and proximal rod within the flagellar motor-hook complex in the CW state.
Keywords keywordsFlagellum, Flagellar motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.27
Radius of gyration Rg (electron density) rg_electron78.54
Forward intensity I(0) i028229700000.00
Molecular weight molecular_weight1409900.0 kDa
Excluded volume excluded_volume1758700 ų
Envelope volume envelope_volume2861100 ų
Hydration-shell volume shell_volume287680 ų
Envelope diameter envelope_diameter255.8
Shell Rg shell_rg88.55
Envelope Rg envelope_rg76.37
Shape Rg shape_rg78.57
Total Rg total_rg78.53
Total atoms total_atoms99073
Residues n_residues12998
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 dmax279.3
Rg (real space) rg_real81.53
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real2.8030e+10
I(0) uncertainty (real space) i0_real_error5.5870e+08
Rg (reciprocal space) rg_reciprocal80.45
I(0) (reciprocal space) i0_reciprocal28320000000.0000
Solution quality estimate total_estimate0.9057
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary97.8
Skewness Skewness skewness0.388
Kurtosis Kurtosis kurtosis0.109
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha1.1600
Highest regularization parameter α highest_alpha5441000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.759; Stabil: 0.909; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)