8uee

Atomic structure of Salmonella SipA/F-actin complex by cryo-EM

Method: ELECTRON MICROSCOPY Dmax: 206.4 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

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 F; UniProt 3–377 Chain H; UniProt 3–377 Chain I; UniProt 3–377 Chain J; UniProt 3–377 Chain K; UniProt 3–377 Chain L; UniProt 3–377 Chain M; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Cell invasion protein SipA × 4 (P0CL52) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 PO4 PHOSPHATE ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;Buffer composition: 25 mM TRIS-H-Cl pH 8.0 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied on Lacey grid, then sample was blotted for 3 seconds and plunge-froze in liquid ethane Resolution 3.20 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–375; UniProt 3–377 Author chain H; PDBConstruct 1–375; UniProt 3–377 Author chain I; PDBConstruct 1–375; UniProt 3–377 Author chain J; PDBConstruct 1–375; UniProt 3–377 Author chain K; PDBConstruct 1–375; UniProt 3–377 Author chain L; PDBConstruct 1–375; UniProt 3–377 Author chain M; PDBConstruct 1–375; UniProt 3–377

Cell invasion protein SipA

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

UniProt P0CL52

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 425–685 Chain B; UniProt 425–685 Chain C; UniProt 425–685 Chain D; UniProt 425–685 Not recorded Actin, alpha skeletal muscle × 7 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 PO4 PHOSPHATE ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;Buffer composition: 25 mM TRIS-H-Cl pH 8.0 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied on Lacey grid, then sample was blotted for 3 seconds and plunge-froze in liquid ethane Resolution 3.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIPA_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–261; UniProt 425–685 Author chain B; PDBConstruct 1–261; UniProt 425–685 Author chain C; PDBConstruct 1–261; UniProt 425–685 Author chain D; PDBConstruct 1–261; UniProt 425–685

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 8uee

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8uee
Deposition date deposition_date2023-10-01
Structure title titleAtomic structure of Salmonella SipA/F-actin complex by cryo-EM
Keywords keywordsactin, Salmonella, type III secretion system, SipA, CELL INVASION; CELL INVASION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.48
Radius of gyration Rg (electron density) rg_electron63.96
Forward intensity I(0) i01983710000.00
Molecular weight molecular_weight369750.0 kDa
Excluded volume excluded_volume461240 ų
Envelope volume envelope_volume637050 ų
Hydration-shell volume shell_volume90709 ų
Envelope diameter envelope_diameter251.1
Shell Rg shell_rg54.91
Envelope Rg envelope_rg64.50
Shape Rg shape_rg63.97
Total Rg total_rg63.70
Total atoms total_atoms25923
Residues n_residues3278
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 dmax206.4
Rg (real space) rg_real63.32
Rg uncertainty (real space) rg_real_error2.00
I(0) (real space) i0_real1.9800e+09
I(0) uncertainty (real space) i0_real_error4.7250e+07
Rg (reciprocal space) rg_reciprocal61.45
I(0) (reciprocal space) i0_reciprocal1976000000.0000
Solution quality estimate total_estimate0.7633
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.637
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0058
Highest regularization parameter α highest_alpha231300000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.624; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.879; Smooth: 0.168

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)