8e5p

Escherichia coli Rho-dependent transcription pre-termination complex containing 24 nt long RNA spacer, Mg-ADP-BeF3, and NusG; Rho hexamer part

Method: ELECTRON MICROSCOPY Dmax: 141.6 Å Quality: EXCELLENT

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

Transcription termination factor Rho

Escherichia coli

UniProt A0A0A0GPI6

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 Homooligomer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain a; UniProt 25–443 Chain b; UniProt 25–443 Chain c; UniProt 25–443 Chain d; UniProt 25–443 Chain e; UniProt 25–443 Chain f; UniProt 25–443 Not recorded RNA with 24 nt long spacer × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0A0GPI6_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–419; UniProt 25–443 Author chain b; PDBConstruct 1–419; UniProt 25–443 Author chain c; PDBConstruct 1–419; UniProt 25–443 Author chain d; PDBConstruct 1–419; UniProt 25–443 Author chain e; PDBConstruct 1–419; UniProt 25–443 Author chain f; PDBConstruct 1–419; UniProt 25–443

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 8e5p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e5p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e5p
Deposition date deposition_date2022-08-22
Structure title titleEscherichia coli Rho-dependent transcription pre-termination complex containing 24 nt long RNA spacer, Mg-ADP-BeF3, and NusG; Rho hexamer part
Keywords keywords;factor-dependent termination, Rho, transcription termination, transcription elongation complex, helicase, ATPase, TRANSCRIPTION-RNA complex ;; TRANSCRIPTION/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.93
Radius of gyration Rg (electron density) rg_electron44.44
Forward intensity I(0) i01220050000.00
Molecular weight molecular_weight286090.0 kDa
Excluded volume excluded_volume357160 ų
Envelope volume envelope_volume508210 ų
Hydration-shell volume shell_volume89678 ų
Envelope diameter envelope_diameter141.1
Shell Rg shell_rg53.77
Envelope Rg envelope_rg44.23
Shape Rg shape_rg44.44
Total Rg total_rg44.81
Total atoms total_atoms20038
Residues n_residues2510
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 dmax141.6
Rg (real space) rg_real44.70
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.2200e+09
I(0) uncertainty (real space) i0_real_error1.9920e+07
Rg (reciprocal space) rg_reciprocal44.93
I(0) (reciprocal space) i0_reciprocal1220000000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.6
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.588
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha135000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)