3j3o

Conformational Shift of a Major Poliovirus Antigen Confirmed by Immuno-Cryogenic Electron Microscopy: 160S Poliovirus and C3-Fab Complex

Method: ELECTRON MICROSCOPY Dmax: 131.8 Å Quality: GOOD

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

Protein VP1

OrganismNot specified

UniProt P03300

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 × 420 PDB declaration: 420-MERIC(420) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 Fragment:UNP residues 2-69 C3 antibody, light chain × 60 C3 antibody, heavy chain × 60 unknown peptide × 60 SPH SPHINGOSINE × 60 MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris, 2 mM CaCl2;pH 7.5;20 mM Tris, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunging;Cryogen ETHANE;Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen. Resolution 11.10 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 Fragment:UNP residues 2-69 C3 antibody, light chain × 1 C3 antibody, heavy chain × 1 unknown peptide × 1 SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris, 2 mM CaCl2;pH 7.5;20 mM Tris, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunging;Cryogen ETHANE;Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen. Resolution 11.10 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 Fragment:UNP residues 2-69 C3 antibody, light chain × 5 C3 antibody, heavy chain × 5 unknown peptide × 5 SPH SPHINGOSINE × 5 MYR MYRISTIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris, 2 mM CaCl2;pH 7.5;20 mM Tris, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunging;Cryogen ETHANE;Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen. Resolution 11.10 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 Fragment:UNP residues 2-69 C3 antibody, light chain × 6 C3 antibody, heavy chain × 6 unknown peptide × 6 SPH SPHINGOSINE × 6 MYR MYRISTIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris, 2 mM CaCl2;pH 7.5;20 mM Tris, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunging;Cryogen ETHANE;Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen. Resolution 11.10 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 Fragment:UNP residues 2-69 C3 antibody, light chain × 1 C3 antibody, heavy chain × 1 unknown peptide × 1 SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:20 mM Tris, 2 mM CaCl2;pH 7.5;20 mM Tris, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunging;Cryogen ETHANE;Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen. Resolution 11.10 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.

80 other PDB entries and 246 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 4, 5, 6, 7
Chains and sequence ranges Author chain 1; PDBConstruct 1–302; UniProt 580–881 Author chain 2; PDBConstruct 1–272; UniProt 70–341 Author chain 3; PDBConstruct 1–238; UniProt 342–579 Author chain 4; PDBConstruct 1–68; UniProt 2–69

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 3j3o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j3o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j3o
Deposition date deposition_date2013-04-10
Structure title titleConformational Shift of a Major Poliovirus Antigen Confirmed by Immuno-Cryogenic Electron Microscopy: 160S Poliovirus and C3-Fab Complex
Keywords keywords;antibody-antigen interaction, antibody-protein interaction, picornavirus, virus-antibody interaction, neutralizing antibody interaction, conformational change, VIRUS-IMMUNE SYSTEM complex ;; VIRUS/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.27
Radius of gyration Rg (electron density) rg_electron39.93
Forward intensity I(0) i0295738000.00
Molecular weight molecular_weight141110.0 kDa
Excluded volume excluded_volume171820 ų
Envelope volume envelope_volume166930 ų
Hydration-shell volume shell_volume37349 ų
Envelope diameter envelope_diameter130.4
Shell Rg shell_rg42.51
Envelope Rg envelope_rg38.01
Shape Rg shape_rg40.07
Total Rg total_rg40.05
Total atoms total_atoms49
Residues n_residues
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 dmax131.8
Rg (real space) rg_real40.40
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real2.9570e+08
I(0) uncertainty (real space) i0_real_error5.0600e+06
Rg (reciprocal space) rg_reciprocal40.27
I(0) (reciprocal space) i0_reciprocal295700000.0000
Solution quality estimate total_estimate0.8667
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.2
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.634
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha39010000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.877; Smooth: 0.766

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)