8ust

In-virion structure of Ebola virus nucleocapsid-like assemblies from recombinant virus-like particles (nucleoprotein, VP24,VP35,VP40)

Method: ELECTRON MICROSCOPY Dmax: 157.2 Å Quality: GOOD

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

Nucleoprotein

Ebola virus - Mayinga, Zaire, 1976

UniProt P18272

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–RNA Heteromer Protein × 7 RNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain A; UniProt 1–739 Chain B; UniProt 1–739 Chain E; UniProt 1–739 Not recorded ;RNA (5'-R(*AP*AP*AP*AP*AP*A)-3') ; × 2 Membrane-associated protein VP24 × 2 (Q05322) Polymerase cofactor VP35 × 2 (Q05127) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCAP_EBOZM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–739; UniProt 1–739 Author chain B; PDBConstruct 1–739; UniProt 1–739 Author chain E; PDBConstruct 1–739; UniProt 1–739

Membrane-associated protein VP24

Ebola virus - Mayinga, Zaire, 1976

UniProt Q05322

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–RNA Heteromer Protein × 7 RNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain I; UniProt 1–251 Chain J; UniProt 1–251 Not recorded Nucleoprotein × 3 (P18272) ;RNA (5'-R(*AP*AP*AP*AP*AP*A)-3') ; × 2 Polymerase cofactor VP35 × 2 (Q05127) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP24_EBOZM
Isoform
PDB entities 3
Chains and sequence ranges Author chain I; PDBConstruct 1–251; UniProt 1–251 Author chain J; PDBConstruct 1–251; UniProt 1–251

Polymerase cofactor VP35

Ebola virus - Mayinga, Zaire, 1976

UniProt Q05127

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–RNA Heteromer Protein × 7 RNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain F; UniProt 1–340 Chain K; UniProt 1–340 Not recorded Nucleoprotein × 3 (P18272) ;RNA (5'-R(*AP*AP*AP*AP*AP*A)-3') ; × 2 Membrane-associated protein VP24 × 2 (Q05322) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.30 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.

25 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35_EBOZM
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–340; UniProt 1–340 Author chain K; PDBConstruct 1–340; UniProt 1–340

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 8ust

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ust
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ust
Deposition date deposition_date2023-10-29
Structure title titleIn-virion structure of Ebola virus nucleocapsid-like assemblies from recombinant virus-like particles (nucleoprotein, VP24,VP35,VP40)
Keywords keywordsVIRAL PROTEIN, nucleoprotein, nucleocapsid, Ebola virus, EBOV, filovirus, subtomogram averaging, in situ, VIRAL PROTEIN-RNA complex; VIRAL PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.34
Radius of gyration Rg (electron density) rg_electron47.71
Forward intensity I(0) i0377070000.00
Molecular weight molecular_weight97713.0 kDa
Excluded volume excluded_volume95977 ų
Envelope volume envelope_volume270280 ų
Hydration-shell volume shell_volume51497 ų
Envelope diameter envelope_diameter161.1
Shell Rg shell_rg46.53
Envelope Rg envelope_rg46.17
Shape Rg shape_rg47.73
Total Rg total_rg47.62
Total atoms total_atoms6954
Residues n_residues1686
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 dmax157.2
Rg (real space) rg_real47.57
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real3.7710e+08
I(0) uncertainty (real space) i0_real_error6.6950e+06
Rg (reciprocal space) rg_reciprocal47.35
I(0) (reciprocal space) i0_reciprocal377000000.0000
Solution quality estimate total_estimate0.8587
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.4
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30030000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.448

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)