8t0l

E. coli Sw2/Snf2 ATPase RapA bound to both ADP-AlF3 and reconstituted E. coli RNA polymerase post-termination complex on negatively-supercoiled DNA

Method: ELECTRON MICROSCOPY Dmax: 180.4 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt C3SR67

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain G; UniProt 4–234 Chain H; UniProt 4–234 Not recorded DNA-directed RNA polymerase subunit beta × 1 (C3SIA7) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit omega × 1 (A7ZTK1) RNA polymerase-associated protein RapA × 1 (B7MAI2) DNA (29-MER) × 1 ;DNA (5'-D(P*TP*CP*TP*GP*AP*AP*TP*TP*TP*AP*AP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SR67_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–231; UniProt 4–234 Author chain H; PDBConstruct 1–231; UniProt 4–234

DNA-directed RNA polymerase subunit beta

Escherichia coli

UniProt C3SIA7

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain I; UniProt 2–1341 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (C3SR67) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit omega × 1 (A7ZTK1) RNA polymerase-associated protein RapA × 1 (B7MAI2) DNA (29-MER) × 1 ;DNA (5'-D(P*TP*CP*TP*GP*AP*AP*TP*TP*TP*AP*AP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SIA7_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–1340; UniProt 2–1341

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

UniProt A0A369F490

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain J; UniProt 16–1373 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (C3SR67) DNA-directed RNA polymerase subunit beta × 1 (C3SIA7) DNA-directed RNA polymerase subunit omega × 1 (A7ZTK1) RNA polymerase-associated protein RapA × 1 (B7MAI2) DNA (29-MER) × 1 ;DNA (5'-D(P*TP*CP*TP*GP*AP*AP*TP*TP*TP*AP*AP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A369F490_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–1358; UniProt 16–1373

DNA-directed RNA polymerase subunit omega

Escherichia coli

UniProt A7ZTK1

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain K; UniProt 3–74 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (C3SR67) DNA-directed RNA polymerase subunit beta × 1 (C3SIA7) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) RNA polymerase-associated protein RapA × 1 (B7MAI2) DNA (29-MER) × 1 ;DNA (5'-D(P*TP*CP*TP*GP*AP*AP*TP*TP*TP*AP*AP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

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

View Construct and Data Evidence
UniProt name RPOZ_ECO24
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–72; UniProt 3–74

RNA polymerase-associated protein RapA

Escherichia coli

UniProt B7MAI2

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain F; UniProt 2–967 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (C3SR67) DNA-directed RNA polymerase subunit beta × 1 (C3SIA7) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit omega × 1 (A7ZTK1) DNA (29-MER) × 1 ;DNA (5'-D(P*TP*CP*TP*GP*AP*AP*TP*TP*TP*AP*AP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.62 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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAPA_ECO45
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–966; UniProt 2–967

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 8t0l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t0l
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8t0l
Deposition date deposition_date2023-06-01
Structure title titleE. coli Sw2/Snf2 ATPase RapA bound to both ADP-AlF3 and reconstituted E. coli RNA polymerase post-termination complex on negatively-supercoiled DNA
Keywords keywords;RNA polymerase, Negatively supercoiled DNA, Sigma-independent transcription, RapA, RNAP recycling, Sw2/Snf2 ATPase, TRANSCRIPTION-DNA complex ;; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.72
Radius of gyration Rg (electron density) rg_electron55.42
Forward intensity I(0) i03442470000.00
Molecular weight molecular_weight478060.0 kDa
Excluded volume excluded_volume593180 ų
Envelope volume envelope_volume873780 ų
Hydration-shell volume shell_volume128370 ų
Envelope diameter envelope_diameter195.5
Shell Rg shell_rg60.15
Envelope Rg envelope_rg54.70
Shape Rg shape_rg55.45
Total Rg total_rg55.45
Total atoms total_atoms33530
Residues n_residues4198
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 dmax180.4
Rg (real space) rg_real55.55
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real3.4420e+09
I(0) uncertainty (real space) i0_real_error7.1570e+07
Rg (reciprocal space) rg_reciprocal55.84
I(0) (reciprocal space) i0_reciprocal3444000000.0000
Solution quality estimate total_estimate0.8715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.9
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha392400000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.682

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)