6n4c

EM structure of the DNA wrapping in bacterial open transcription initiation complex

Method: ELECTRON MICROSCOPY Dmax: 182.1 Å Quality: GOOD

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

RNA polymerase sigma factor RpoD

OrganismNot specified

UniProt P00579

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 8–613 Not recorded DNA-directed RNA polymerase subunit beta × 1 (A0A0A0GWV9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (94-MER) × 1 DNA (94-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 Resolution 17.00 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.

91 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–558; UniProt 8–613

DNA-directed RNA polymerase subunit beta

OrganismNot specified

UniProt A0A0A0GWV9

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 C; UniProt 13–1353 Not recorded RNA polymerase sigma factor RpoD × 1 (P00579) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (94-MER) × 1 DNA (94-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 Resolution 17.00 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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0A0GWV9_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1341; UniProt 13–1353

;DNA-directed RNA polymerase subunit beta' ;

OrganismNot specified

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 D; UniProt 15–1376 Not recorded RNA polymerase sigma factor RpoD × 1 (P00579) DNA-directed RNA polymerase subunit beta × 1 (A0A0A0GWV9) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (94-MER) × 1 DNA (94-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 Resolution 17.00 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 D; PDBConstruct 1–1358; UniProt 15–1376

DNA-directed RNA polymerase subunit alpha

OrganismNot specified

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 × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 6–321 Chain B; UniProt 6–315 Not recorded RNA polymerase sigma factor RpoD × 1 (P00579) DNA-directed RNA polymerase subunit beta × 1 (A0A0A0GWV9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (94-MER) × 1 DNA (94-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 Resolution 17.00 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 4, 5
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 6–321 Author chain B; PDBConstruct 1–310; UniProt 6–315

DNA-directed RNA polymerase subunit omega

OrganismNot specified

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 × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain E; UniProt 2–91 Not recorded RNA polymerase sigma factor RpoD × 1 (P00579) DNA-directed RNA polymerase subunit beta × 1 (A0A0A0GWV9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A369F490) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA-directed RNA polymerase subunit alpha × 1 (P0A7Z4) DNA (94-MER) × 1 DNA (94-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 Resolution 17.00 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 6
Chains and sequence ranges Author chain E; PDBConstruct 1–90; UniProt 2–91

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 6n4c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n4c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n4c
Deposition date deposition_date2018-11-19
Structure title titleEM structure of the DNA wrapping in bacterial open transcription initiation complex
Keywords keywords;DNA wrapping, bacterial transcription initiation complex, transmission electron microscopy, single particle analysis., TRANSCRIPTION, 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_guinier54.70
Radius of gyration Rg (electron density) rg_electron53.54
Forward intensity I(0) i04223010000.00
Molecular weight molecular_weight502530.0 kDa
Excluded volume excluded_volume611860 ų
Envelope volume envelope_volume921370 ų
Hydration-shell volume shell_volume135910 ų
Envelope diameter envelope_diameter182.3
Shell Rg shell_rg61.40
Envelope Rg envelope_rg53.29
Shape Rg shape_rg53.51
Total Rg total_rg53.81
Total atoms total_atoms68774
Residues n_residues4161
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 dmax182.1
Rg (real space) rg_real54.51
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real4.2230e+09
I(0) uncertainty (real space) i0_real_error8.9680e+07
Rg (reciprocal space) rg_reciprocal54.85
I(0) (reciprocal space) i0_reciprocal4225000000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.1
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha534800000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)