9mse

de novo SigN RNA polymerase transcription initiation intermediate with pre-catalytic bEBP state (RPi1 open ring)

Method: ELECTRON MICROSCOPY Dmax: 255.3 Å Quality: GOOD

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

Transcriptional regulator (NtrC family)

Aquifex aeolicus VF5

UniProt O67198

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 × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain A; UniProt 121–387 Chain B; UniProt 121–387 Chain C; UniProt 121–387 Chain D; UniProt 121–387 Chain E; UniProt 121–387 Chain F; UniProt 121–387 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma-54 factor × 1 (P24255) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O67198_AQUAE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–268; UniProt 121–387 Author chain B; PDBConstruct 2–268; UniProt 121–387 Author chain C; PDBConstruct 2–268; UniProt 121–387 Author chain D; PDBConstruct 2–268; UniProt 121–387 Author chain E; PDBConstruct 2–268; UniProt 121–387 Author chain F; PDBConstruct 2–268; UniProt 121–387

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 Protein–DNA Heteromer Protein × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain G; UniProt 1–329 Chain H; UniProt 1–329 Not recorded Transcriptional regulator (NtrC family) × 6 (O67198) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma-54 factor × 1 (P24255) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 2
Chains and sequence ranges Author chain G; PDBConstruct 1–329; UniProt 1–329 Author chain H; PDBConstruct 1–329; UniProt 1–329

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 Protein–DNA Heteromer Protein × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain I; UniProt 1–1342 Not recorded Transcriptional regulator (NtrC family) × 6 (O67198) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma-54 factor × 1 (P24255) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 3
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 Protein–DNA Heteromer Protein × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain J; UniProt 1–1407 Not recorded Transcriptional regulator (NtrC family) × 6 (O67198) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma-54 factor × 1 (P24255) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 4
Chains and sequence ranges Author chain J; PDBConstruct 1–1407; UniProt 1–1407

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 Protein–DNA Heteromer Protein × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain K; UniProt 1–91 Not recorded Transcriptional regulator (NtrC family) × 6 (O67198) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma-54 factor × 1 (P24255) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 5
Chains and sequence ranges Author chain K; PDBConstruct 1–91; UniProt 1–91

RNA polymerase sigma-54 factor

Escherichia coli

UniProt P24255

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 × 12 DNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain M; UniProt 1–477 Not recorded Transcriptional regulator (NtrC family) × 6 (O67198) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) dhsU (-60 to +30) non-template strand × 2 dhsU (-60 to +30) template strand × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 3 POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;40 mM Tris-HCl, pH 8/RT, 200 mM KCl, 10 mM MgCl2, 1 mM DTT; fluorinated fos-choline-8 (FC8F) added to a final concentration of 1.5 mM during grid preparation cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RP54_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain M; PDBConstruct 1–477; UniProt 1–477

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 9mse

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mse
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mse
Deposition date deposition_date2025-01-09
最后修订 last_revision2025-08-13
Structure title titlede novo SigN RNA polymerase transcription initiation intermediate with pre-catalytic bEBP state (RPi1 open ring)
Keywords keywordssigma N, sigma 54, ATPase, bacterial enhancer binding protein, transcription initiation, intermediate, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier66.51
Radius of gyration Rg (electron density) rg_electron67.21
Forward intensity I(0) i05582130000.00
Molecular weight molecular_weight614970.0 kDa
Excluded volume excluded_volume764130 ų
Envelope volume envelope_volume1234200 ų
Hydration-shell volume shell_volume154740 ų
Envelope diameter envelope_diameter240.2
Shell Rg shell_rg67.02
Envelope Rg envelope_rg65.12
Shape Rg shape_rg67.23
Total Rg total_rg67.16
Total atoms total_atoms43107
Residues n_residues5292
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 dmax255.3
Rg (real space) rg_real70.96
Rg uncertainty (real space) rg_real_error1.73
I(0) (real space) i0_real5.6410e+09
I(0) uncertainty (real space) i0_real_error1.1710e+08
Rg (reciprocal space) rg_reciprocal66.37
I(0) (reciprocal space) i0_reciprocal5579000000.0000
Solution quality estimate total_estimate0.8590
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.5
Skewness Skewness skewness0.656
Kurtosis Kurtosis kurtosis0.235
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.9156
Highest regularization parameter α highest_alpha664600000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.637; Stabil: 0.837; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)