9vui

Cryo-EM structure of the human measles virus RNA-dependent RNA polymerase complex bound to viral protein C

Method: ELECTRON MICROSCOPY Dmax: 148.7 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Phosphoprotein

Measles virus genotype A-vaccine

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 29–392 Chain B; UniProt 29–392 Chain C; UniProt 29–392 Chain D; UniProt 29–392 Chain L; UniProt 29–392 Chain X; UniProt 29–392 Chain Y; UniProt 29–392 Not recorded ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;300mM NaCl, 25mM HEPES, 1mM TCEP, 6mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 15–378; UniProt 29–392 Author chain B; PDBConstruct 15–378; UniProt 29–392 Author chain C; PDBConstruct 15–378; UniProt 29–392 Author chain D; PDBConstruct 15–378; UniProt 29–392 Author chain L; PDBConstruct 15–378; UniProt 29–392 Author chain X; PDBConstruct 15–378; UniProt 29–392 Author chain Y; PDBConstruct 15–378; UniProt 29–392

Maltose/maltodextrin-binding periplasmic protein,Phosphoprotein

Measles virus genotype A-vaccine

UniProt P35974

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 304–507 Chain B; UniProt 304–507 Chain C; UniProt 304–507 Chain D; UniProt 304–507 Not recorded Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L,Strep II and FLAG tag × 1 (P0AEX9,P35975) Maltose/maltodextrin-binding periplasmic protein,Protein C,Green fluorescent protein × 2 (P0AEX9,P35977,P42212) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;300mM NaCl, 25mM HEPES, 1mM TCEP, 6mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHOSP_MEASA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 399–602; UniProt 304–507 Author chain B; PDBConstruct 399–602; UniProt 304–507 Author chain C; PDBConstruct 399–602; UniProt 304–507 Author chain D; PDBConstruct 399–602; UniProt 304–507

Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L,Strep II and FLAG tag

synthetic construct

UniProt P35975

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain L; UniProt 1–2183 Not recorded Maltose/maltodextrin-binding periplasmic protein,Phosphoprotein × 4 (P0AEX9,P35974) Maltose/maltodextrin-binding periplasmic protein,Protein C,Green fluorescent protein × 2 (P0AEX9,P35977,P42212) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;300mM NaCl, 25mM HEPES, 1mM TCEP, 6mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L_MEASA
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 399–2581; UniProt 1–2183

Maltose/maltodextrin-binding periplasmic protein,Protein C,Green fluorescent protein

Aequorea victoria

UniProt P35977

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain X; UniProt 1–186 Chain Y; UniProt 1–186 Not recorded Maltose/maltodextrin-binding periplasmic protein,Phosphoprotein × 4 (P0AEX9,P35974) Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L,Strep II and FLAG tag × 1 (P0AEX9,P35975) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;300mM NaCl, 25mM HEPES, 1mM TCEP, 6mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name C_MEASA
Isoform
PDB entities 3
Chains and sequence ranges Author chain X; PDBConstruct 399–584; UniProt 1–186 Author chain Y; PDBConstruct 399–584; UniProt 1–186

Maltose/maltodextrin-binding periplasmic protein,Protein C,Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain X; UniProt 1–238 Chain Y; UniProt 1–238 Not recorded Maltose/maltodextrin-binding periplasmic protein,Phosphoprotein × 4 (P0AEX9,P35974) Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L,Strep II and FLAG tag × 1 (P0AEX9,P35975) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;300mM NaCl, 25mM HEPES, 1mM TCEP, 6mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 3
Chains and sequence ranges Author chain X; PDBConstruct 600–838; UniProt 1–238 Author chain Y; PDBConstruct 600–838; UniProt 1–238

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 9vui

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vui
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vui
Deposition date deposition_date2025-07-13
Structure title titleCryo-EM structure of the human measles virus RNA-dependent RNA polymerase complex bound to viral protein C
Keywords keywordsMeasles virus RNA-dependent RNA polymerase complex bound to viral protein C, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.08
Radius of gyration Rg (electron density) rg_electron45.68
Forward intensity I(0) i01052150000.00
Molecular weight molecular_weight276530.0 kDa
Excluded volume excluded_volume349920 ų
Envelope volume envelope_volume499860 ų
Hydration-shell volume shell_volume89925 ų
Envelope diameter envelope_diameter158.7
Shell Rg shell_rg51.91
Envelope Rg envelope_rg44.32
Shape Rg shape_rg45.67
Total Rg total_rg45.99
Total atoms total_atoms19432
Residues n_residues2440
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 dmax148.7
Rg (real space) rg_real45.92
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.0520e+09
I(0) uncertainty (real space) i0_real_error1.8730e+07
Rg (reciprocal space) rg_reciprocal46.08
I(0) (reciprocal space) i0_reciprocal1052000000.0000
Solution quality estimate total_estimate0.8827
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.8
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha107600000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.842

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)