8zdu

Structure of the RBM3 ring of Salmonella flagellar MS-ring protein FliF with C34 symmetry applied

Method: ELECTRON MICROSCOPY Dmax: 257.2 Å Quality: REASONABLE

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

Flagellar M-ring protein

Salmonella enterica subsp. enterica serovar Typhimurium

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 homooligomer Homooligomer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain A; 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 M; UniProt 1–560 Chain N; UniProt 1–560 Chain O; UniProt 1–560 Chain P; UniProt 1–560 Chain Q; UniProt 1–560 Chain R; UniProt 1–560 Chain S; 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 Chain a; 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 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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 A; 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 M; PDBConstruct 1–560; UniProt 1–560 Author chain N; PDBConstruct 1–560; UniProt 1–560 Author chain O; PDBConstruct 1–560; UniProt 1–560 Author chain P; PDBConstruct 1–560; UniProt 1–560 Author chain Q; PDBConstruct 1–560; UniProt 1–560 Author chain R; PDBConstruct 1–560; UniProt 1–560 Author chain S; 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 Author chain a; 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

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 8zdu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8zdu
Deposition date deposition_date2024-05-03
Structure title titleStructure of the RBM3 ring of Salmonella flagellar MS-ring protein FliF with C34 symmetry applied
Keywords keywordsBacterial flagellum, flagellar assembly, electron Cryomicroscopy, MS-ring, type III secretion system, Salmonella, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier87.84
Radius of gyration Rg (electron density) rg_electron88.89
Forward intensity I(0) i05548620000.00
Molecular weight molecular_weight595660.0 kDa
Excluded volume excluded_volume731820 ų
Envelope volume envelope_volume1593900 ų
Hydration-shell volume shell_volume159740 ų
Envelope diameter envelope_diameter250.8
Shell Rg shell_rg88.80
Envelope Rg envelope_rg77.36
Shape Rg shape_rg88.86
Total Rg total_rg88.99
Total atoms total_atoms41854
Residues n_residues5304
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 dmax257.2
Rg (real space) rg_real87.62
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real5.5490e+09
I(0) uncertainty (real space) i0_real_error1.1780e+08
Rg (reciprocal space) rg_reciprocal88.74
I(0) (reciprocal space) i0_reciprocal5563000000.0000
Solution quality estimate total_estimate0.6066
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary142.9
Skewness Skewness skewness-0.072
Kurtosis Kurtosis kurtosis-0.803
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.0758
Highest regularization parameter α highest_alpha162800000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 0.999; Sysdev: 0.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)