4d5y

Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated state

Method: ELECTRON MICROSCOPY Dmax: 291.5 Å Quality: GOOD

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

60S RIBOSOMAL PROTEIN UL2

OrganismNot specified

UniProt G1TT27

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 × 43 RNA 3 PDB declaration: 46-meric(46) Consistent with all polymer counts Chain A; UniProt 1–257 Not recorded 60S RIBOSOMAL PROTEIN UL3 × 1 60S RIBOSOMAL PROTEIN UL4 × 1 60S RIBOSOMAL PROTEIN UL18 × 1 60S RIBOSOMAL PROTEIN EL6 × 1 60S RIBOSOMAL PROTEIN UL30 × 1 60S RIBOSOMAL PROTEIN EL8 × 1 60S RIBOSOMAL PROTEIN UL6 × 1 60S RIBOSOMAL PROTEIN UL16 × 1 60S RIBOSOMAL PROTEIN UL5 × 1 60S RIBOSOMAL PROTEIN EL13 × 1 60S RIBOSOMAL PROTEIN EL14 × 1 60S RIBOSOMAL PROTEIN EL15 × 1 60S RIBOSOMAL PROTEIN UL13 × 1 60S RIBOSOMAL PROTEIN UL22 × 1 60S RIBOSOMAL PROTEIN EL18 × 1 60S RIBOSOMAL PROTEIN UL19 × 1 60S RIBOSOMAL PROTEIN EL20 × 1 60S RIBOSOMAL PROTEIN EL21 × 1 60S RIBOSOMAL PROTEIN EL22 × 1 60S RIBOSOMAL PROTEIN UL14 × 1 60S RIBOSOMAL PROTEIN EL24 × 1 60S RIBOSOMAL PROTEIN UL23 × 1 60S RIBOSOMAL PROTEIN UL24 × 1 60S RIBOSOMAL PROTEIN EL27 × 1 60S RIBOSOMAL PROTEIN UL15 × 1 60S RIBOSOMAL PROTEIN EL29 × 1 60S RIBOSOMAL PROTEIN EL30 × 1 60S RIBOSOMAL PROTEIN EL31 × 1 60S RIBOSOMAL PROTEIN EL32 × 1 60S RIBOSOMAL PROTEIN EL33 × 1 60S RIBOSOMAL PROTEIN EL34 × 1 60S RIBOSOMAL PROTEIN UL29 × 1 60S RIBOSOMAL PROTEIN EL36 × 1 60S RIBOSOMAL PROTEIN EL37 × 1 60S RIBOSOMAL PROTEIN EL38 × 1 60S RIBOSOMAL PROTEIN EL39 × 1 60S RIBOSOMAL PROTEIN EL40 × 1 60S RIBOSOMAL PROTEIN EL41 × 1 60S RIBOSOMAL PROTEIN EL44 × 1 60S RIBOSOMAL PROTEIN EL43 × 1 60S RIBOSOMAL PROTEIN EL28 × 1 60S RIBOSOMAL PROTEIN UL1 × 1 28S Ribosomal RNA × 1 5.8S Ribosomal RNA × 1 5S Ribosomal RNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:20 MM TRIS PH 7.5, 100 MM KCL, 1 MM DTT, 2.5 MM MGCL2, 0.5 MM GTP;pH 7.5;20 MM TRIS PH 7.5, 100 MM KCL, 1 MM DTT, 2.5 MM MGCL2, 0.5 MM GTP cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 9.00 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 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G1TT27_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–257; UniProt 1–257

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 4d5y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4d5y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4d5y
Deposition date deposition_date2014-11-07
Structure title titleCryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated state
Keywords keywordsCRPV IRES, RIBOSOME, TERMINATION, RELEASE FACTORS; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier80.11
Radius of gyration Rg (electron density) rg_electron80.64
Forward intensity I(0) i0122487000000.00
Molecular weight molecular_weight2019900.0 kDa
Excluded volume excluded_volume2130400 ų
Envelope volume envelope_volume3587200 ų
Hydration-shell volume shell_volume334480 ų
Envelope diameter envelope_diameter279.2
Shell Rg shell_rg95.56
Envelope Rg envelope_rg81.16
Shape Rg shape_rg80.66
Total Rg total_rg80.67
Total atoms total_atoms136495
Residues n_residues10459
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 dmax291.5
Rg (real space) rg_real82.99
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real1.2220e+11
I(0) uncertainty (real space) i0_real_error2.7880e+09
Rg (reciprocal space) rg_reciprocal80.98
I(0) (reciprocal space) i0_reciprocal122800000000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary92.0
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis0.248
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha1.0350
Highest regularization parameter α highest_alpha13410000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 0.902; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.783

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (46)

8. Citations (1)

9. Files and Curves (10)