10mb

Open1 Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with an open active site (open TL, SI3 and RH-FL)

Method: ELECTRON MICROSCOPY Dmax: 159.3 Å Quality: REASONABLE

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

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain K; UniProt 1–91 Not recorded DNA × 1 ;RNA (5'-R(P*GP*AP*UP*GP*UP*GP*UP*GP*CP*U)-3') ; × 1 ;DNA (5'-D(*CP*GP*TP*CP*CP*TP*TP*TP*CP*GP*GP*AP*AP*GP*AP*GP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) 1N7 CHAPSO × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 2
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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain G; UniProt 1–329 Chain H; UniProt 1–329 Not recorded DNA × 1 DNA-directed RNA polymerase subunit omega × 1 (P0A800) ;RNA (5'-R(P*GP*AP*UP*GP*UP*GP*UP*GP*CP*U)-3') ; × 1 ;DNA (5'-D(*CP*GP*TP*CP*CP*TP*TP*TP*CP*GP*GP*AP*AP*GP*AP*GP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) 1N7 CHAPSO × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain I; UniProt 1–1342 Not recorded DNA × 1 DNA-directed RNA polymerase subunit omega × 1 (P0A800) ;RNA (5'-R(P*GP*AP*UP*GP*UP*GP*UP*GP*CP*U)-3') ; × 1 ;DNA (5'-D(*CP*GP*TP*CP*CP*TP*TP*TP*CP*GP*GP*AP*AP*GP*AP*GP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) 1N7 CHAPSO × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 6
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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain J; UniProt 1–1407 Not recorded DNA × 1 DNA-directed RNA polymerase subunit omega × 1 (P0A800) ;RNA (5'-R(P*GP*AP*UP*GP*UP*GP*UP*GP*CP*U)-3') ; × 1 ;DNA (5'-D(*CP*GP*TP*CP*CP*TP*TP*TP*CP*GP*GP*AP*AP*GP*AP*GP*AP*TP*TP*CP*AP*GP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) 1N7 CHAPSO × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 7
Chains and sequence ranges Author chain J; PDBConstruct 1–1407; UniProt 1–1407

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 10mb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10mb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10mb
Deposition date deposition_date2026-01-27
Structure title titleOpen1 Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with an open active site (open TL, SI3 and RH-FL)
Keywords keywordsTranscription, Nucleotide addition cycle, DNA/RNA, TRANSCRIPTION-DNA-RNA complex; TRANSCRIPTION/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.03
Radius of gyration Rg (electron density) rg_electron48.78
Forward intensity I(0) i02167390000.00
Molecular weight molecular_weight372730.0 kDa
Excluded volume excluded_volume460880 ų
Envelope volume envelope_volume698750 ų
Hydration-shell volume shell_volume113660 ų
Envelope diameter envelope_diameter168.6
Shell Rg shell_rg56.76
Envelope Rg envelope_rg48.47
Shape Rg shape_rg48.79
Total Rg total_rg48.99
Total atoms total_atoms26093
Residues n_residues3231
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 dmax159.3
Rg (real space) rg_real48.79
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real2.1670e+09
I(0) uncertainty (real space) i0_real_error3.8550e+07
Rg (reciprocal space) rg_reciprocal49.03
I(0) (reciprocal space) i0_reciprocal2168000000.0000
Solution quality estimate total_estimate0.6616
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha509400000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 0.087; Positv: 1.000; Valcen: 0.973; Smooth: 0.837

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)