8phk

fully recruited RfaH bound to E. coli transcription complex paused at ops site

Method: ELECTRON MICROSCOPY Dmax: 158.0 Å Quality: GOOD

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

Transcription antitermination protein RfaH

Escherichia coli

UniProt P0AFW0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain P; UniProt 1–162 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) non-template DNA × 1 template DNA × 1 RNA × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFAH_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 3–164; UniProt 1–162

DNA-directed RNA polymerase subunit beta

Escherichia coli

UniProt P0A8V2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain I; UniProt 1–1342 Not recorded Transcription antitermination protein RfaH × 1 (P0AFW0) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) non-template DNA × 1 template DNA × 1 RNA × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

219 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

UniProt P0A8T7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain J; UniProt 2–1407 Not recorded Transcription antitermination protein RfaH × 1 (P0AFW0) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) non-template DNA × 1 template DNA × 1 RNA × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

239 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 2–1407; UniProt 2–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli

UniProt P0A800

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain K; UniProt 1–91 Not recorded Transcription antitermination protein RfaH × 1 (P0AFW0) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) non-template DNA × 1 template DNA × 1 RNA × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

258 other PDB entries and 277 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–91; UniProt 1–91

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt P0A7Z4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain G; UniProt 1–329 Chain H; UniProt 1–329 Not recorded Transcription antitermination protein RfaH × 1 (P0AFW0) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) non-template DNA × 1 template DNA × 1 RNA × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

276 other PDB entries and 305 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–329; UniProt 1–329 Author chain H; PDBConstruct 1–329; UniProt 1–329

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 8phk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8phk
Deposition date deposition_date2023-06-20
最后修订 last_revision2024-04-24
Structure title titlefully recruited RfaH bound to E. coli transcription complex paused at ops site
Keywords keywordspausing, RfaH, ops site, transcription complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.88
Radius of gyration Rg (electron density) rg_electron48.72
Forward intensity I(0) i02583940000.00
Molecular weight molecular_weight403250.0 kDa
Excluded volume excluded_volume496550 ų
Envelope volume envelope_volume708800 ų
Hydration-shell volume shell_volume115210 ų
Envelope diameter envelope_diameter164.3
Shell Rg shell_rg56.91
Envelope Rg envelope_rg48.34
Shape Rg shape_rg48.74
Total Rg total_rg48.91
Total atoms total_atoms28209
Residues n_residues3458
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 dmax158.0
Rg (real space) rg_real48.63
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real2.5840e+09
I(0) uncertainty (real space) i0_real_error4.5030e+07
Rg (reciprocal space) rg_reciprocal48.87
I(0) (reciprocal space) i0_reciprocal2585000000.0000
Solution quality estimate total_estimate0.8731
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.2
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha640000000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.809

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)