2om7

Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors

Method: ELECTRON MICROSCOPY Dmax: 244.5 Å Quality: GOOD

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

30S ribosomal protein S12

OrganismNot specified

UniProt P17293

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 × 4 RNA 10 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain E; UniProt 1–132 Not recorded Fragment of 16S rRNA (h14) × 1 Fragment of 16S rRNA (h15) × 1 Fragment of 16S rRNA (h44) × 1 16S ribosomal RNA (H5) × 1 Fragment of23S rRNA (H95) × 1 Fragment of23S rRNA (H68) × 1 Fragment of23S rRNA (H89) × 1 Fragment of23S rRNA (H42-44) × 1 Fragment of23S rRNA (H76) × 1 p/E-tRNA × 1 50S ribosomal protein L1 × 1 (Q5SLP7) Elongation factor G × 1 (P13551) 30S ribosomal protein S2 × 1 (P80371) ELECTRON MICROSCOPY cryo-EM buffer:0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol;pH 7.8;0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol 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.

35 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS12_THETH
Isoform
PDB entities 11
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 1–132

50S ribosomal protein L1

OrganismNot specified

UniProt Q5SLP7

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 × 4 RNA 10 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain K; UniProt 1–229 Not recorded Fragment of 16S rRNA (h14) × 1 Fragment of 16S rRNA (h15) × 1 Fragment of 16S rRNA (h44) × 1 16S ribosomal RNA (H5) × 1 Fragment of23S rRNA (H95) × 1 Fragment of23S rRNA (H68) × 1 Fragment of23S rRNA (H89) × 1 Fragment of23S rRNA (H42-44) × 1 Fragment of23S rRNA (H76) × 1 p/E-tRNA × 1 30S ribosomal protein S12 × 1 (P17293) Elongation factor G × 1 (P13551) 30S ribosomal protein S2 × 1 (P80371) ELECTRON MICROSCOPY cryo-EM buffer:0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol;pH 7.8;0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol 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.

53 other PDB entries and 84 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL1_THET8
Isoform
PDB entities 12
Chains and sequence ranges Author chain K; PDBConstruct 1–229; UniProt 1–229

Elongation factor G

Thermus thermophilus

UniProt P13551

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 × 4 RNA 10 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 1–691 Not recorded Fragment of 16S rRNA (h14) × 1 Fragment of 16S rRNA (h15) × 1 Fragment of 16S rRNA (h44) × 1 16S ribosomal RNA (H5) × 1 Fragment of23S rRNA (H95) × 1 Fragment of23S rRNA (H68) × 1 Fragment of23S rRNA (H89) × 1 Fragment of23S rRNA (H42-44) × 1 Fragment of23S rRNA (H76) × 1 p/E-tRNA × 1 30S ribosomal protein S12 × 1 (P17293) 50S ribosomal protein L1 × 1 (Q5SLP7) 30S ribosomal protein S2 × 1 (P80371) ELECTRON MICROSCOPY cryo-EM buffer:0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol;pH 7.8;0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFG_THETH
Isoform
PDB entities 13
Chains and sequence ranges Author chain L; PDBConstruct 1–691; UniProt 1–691

30S ribosomal protein S2

OrganismNot specified

UniProt P80371

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 × 4 RNA 10 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain N; UniProt 1–256 Not recorded Fragment of 16S rRNA (h14) × 1 Fragment of 16S rRNA (h15) × 1 Fragment of 16S rRNA (h44) × 1 16S ribosomal RNA (H5) × 1 Fragment of23S rRNA (H95) × 1 Fragment of23S rRNA (H68) × 1 Fragment of23S rRNA (H89) × 1 Fragment of23S rRNA (H42-44) × 1 Fragment of23S rRNA (H76) × 1 p/E-tRNA × 1 30S ribosomal protein S12 × 1 (P17293) 50S ribosomal protein L1 × 1 (Q5SLP7) Elongation factor G × 1 (P13551) ELECTRON MICROSCOPY cryo-EM buffer:0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol;pH 7.8;0.3 mM GMPPNP, 10 mM Hepes-KOH (pH 7.8), 10 mM Mg acetate, 60 mM NH4Cl, and 6 mM B-mercaptoethanol 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.

375 other PDB entries and 595 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS2_THET8
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–256; UniProt 1–256

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 2om7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2om7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2om7
Deposition date deposition_date2007-01-21
Structure title titleStructural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors
Keywords keywordsRNA-Protein Complex, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.31
Radius of gyration Rg (electron density) rg_electron72.07
Forward intensity I(0) i02196910000.00
Molecular weight molecular_weight279620.0 kDa
Excluded volume excluded_volume302280 ų
Envelope volume envelope_volume658940 ų
Hydration-shell volume shell_volume83128 ų
Envelope diameter envelope_diameter222.7
Shell Rg shell_rg61.96
Envelope Rg envelope_rg68.17
Shape Rg shape_rg72.13
Total Rg total_rg71.78
Total atoms total_atoms19031
Residues n_residues1659
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 dmax244.5
Rg (real space) rg_real71.47
Rg uncertainty (real space) rg_real_error2.36
I(0) (real space) i0_real2.1980e+09
I(0) uncertainty (real space) i0_real_error5.1020e+07
Rg (reciprocal space) rg_reciprocal70.89
I(0) (reciprocal space) i0_reciprocal2195000000.0000
Solution quality estimate total_estimate0.8702
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary66.7
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.868
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0184
Highest regularization parameter α highest_alpha55820000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2om7e1
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.1 — Ribosome complexes
Domain ID domain_idd2om7k1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.24 — Ribosomal protein L1
Superfamily Superfamily superfamilye.24.1 — Ribosomal protein L1
Family Family familye.24.1.1 — Ribosomal protein L1
Domain ID domain_idd2om7n1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.15 — Ribosomal protein S2
Family Family familyc.23.15.1 — Ribosomal protein S2

8. Citations (1)

9. Files and Curves (10)