2vrh

Structure of the E. coli trigger factor bound to a translating ribosome

Method: ELECTRON MICROSCOPY Dmax: 128.8 Å Quality: GOOD

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

TRIGGER FACTOR

ESCHERICHIA COLI

UniProt P0A850

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–432 Non-standard monomer:Yes (specific site not provided by mmCIF) 50S RIBOSOMAL PROTEIN L23 × 1 (Q0TCE3) 50S RIBOSOMAL PROTEIN L24 × 1 (P60624) 50S RIBOSOMAL PROTEIN L29 × 1 (P0A7M6) ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL;pH 7.5;50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 19.00 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.

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIG_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–432; UniProt 1–432

50S RIBOSOMAL PROTEIN L23

OrganismNot specified

UniProt Q0TCE3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–100 Not recorded TRIGGER FACTOR × 1 (P0A850) 50S RIBOSOMAL PROTEIN L24 × 1 (P60624) 50S RIBOSOMAL PROTEIN L29 × 1 (P0A7M6) ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL;pH 7.5;50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 19.00 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.

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

View Construct and Data Evidence
UniProt name RL23_ECOL5
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–100; UniProt 1–100

50S RIBOSOMAL PROTEIN L24

OrganismNot specified

UniProt P60624

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–104 Fragment:RESIDUES 2-104 TRIGGER FACTOR × 1 (P0A850) 50S RIBOSOMAL PROTEIN L23 × 1 (Q0TCE3) 50S RIBOSOMAL PROTEIN L29 × 1 (P0A7M6) ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL;pH 7.5;50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 19.00 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.

452 other PDB entries and 496 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL24_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–103; UniProt 2–104

50S RIBOSOMAL PROTEIN L29

OrganismNot specified

UniProt P0A7M6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–63 Not recorded TRIGGER FACTOR × 1 (P0A850) 50S RIBOSOMAL PROTEIN L23 × 1 (Q0TCE3) 50S RIBOSOMAL PROTEIN L24 × 1 (P60624) ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL;pH 7.5;50 MM HEPES-KOH PH 7.5, 100 MM KCL, 25 MM MGCL2, 0.5 MG/ML CHLORAMPHENICOL cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 19.00 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.

457 other PDB entries and 502 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL29_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–63; UniProt 1–63

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 2vrh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2vrh
Deposition date deposition_date2008-04-07
Structure title titleStructure of the E. coli trigger factor bound to a translating ribosome
Keywords keywords;RIBOSOME, TRIGGER FACTOR, RIBOSOMAL PROTEIN, RIBONUCLEOPROTEIN, CO-TRANSLATIONAL PROTEIN FOLDING, ROTAMASE, CHAPERONE, ISOMERASE, CELL CYCLE, RNA-BINDING, RRNA-BINDING, CELL DIVISION, RIBOSOME-NASCENT CHAIN COMPLEX ;; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.19
Radius of gyration Rg (electron density) rg_electron42.10
Forward intensity I(0) i086713200.00
Molecular weight molecular_weight76222.0 kDa
Excluded volume excluded_volume93656 ų
Envelope volume envelope_volume112080 ų
Hydration-shell volume shell_volume24621 ų
Envelope diameter envelope_diameter125.1
Shell Rg shell_rg43.35
Envelope Rg envelope_rg37.76
Shape Rg shape_rg42.02
Total Rg total_rg42.17
Total atoms total_atoms11
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 dmax128.8
Rg (real space) rg_real42.22
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real8.6710e+07
I(0) uncertainty (real space) i0_real_error1.6260e+06
Rg (reciprocal space) rg_reciprocal42.19
I(0) (reciprocal space) i0_reciprocal86710000.0000
Solution quality estimate total_estimate0.8480
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.648
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4046000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.994; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.056

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2vrha1
Class classa — All alpha proteins
Fold Fold folda.223 — Triger factor/SurA peptide-binding domain-like
Superfamily Superfamily superfamilya.223.1 — Triger factor/SurA peptide-binding domain-like
Family Family familya.223.1.1 — TF C-terminus
Domain ID domain_idd2vrha2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.241 — Ribosome binding domain-like
Superfamily Superfamily superfamilyd.241.2 — Trigger factor ribosome-binding domain
Family Family familyd.241.2.1 — Trigger factor ribosome-binding domain
Domain ID domain_idd2vrha3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.26 — FKBP-like
Superfamily Superfamily superfamilyd.26.1 — FKBP-like
Family Family familyd.26.1.1 — FKBP immunophilin/proline isomerase
Domain ID domain_idd2vrhb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.12 — Ribosomal proteins S24e, L23 and L15e
Superfamily Superfamily superfamilyd.12.1 — Ribosomal proteins S24e, L23 and L15e
Family Family familyd.12.1.1 — L23p
Domain ID domain_idd2vrhc1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.5 — Translation proteins SH3-like domain
Family Family familyb.34.5.1 — Ribosomal proteins L24p and L21e
Domain ID domain_idd2vrhd1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.2 — Ribosomal protein L29 (L29p)
Family Family familya.2.2.1 — Ribosomal protein L29 (L29p)

8. Citations (1)

9. Files and Curves (10)