6uu8

E. coli mutant sigma-S transcription initiation complex with a 7-nt RNA ("Fresh" mutant crystal soaked with GTP, UTP, and CTP for 30 minutes)

Method: X-RAY DIFFRACTION Dmax: 157.7 Å Quality: REASONABLE

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

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 AAA; UniProt 1–235 Chain BBB; UniProt 1–235 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoS × 1 (A0A377K1M2) Synthetic DNA 50-mer (promoter non-template strand) × 1 Synthetic DNA 50-mer (promoter template strand) × 1 RNA 7-mer (de novo synthesized) × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 DPO DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;PEG3350, sodium chloride, HEPES Resolution 4.40 Å R-free 0.380

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 1
Chains and sequence ranges Author chain AAA; PDBConstruct 8–242; UniProt 1–235 Author chain BBB; PDBConstruct 8–242; UniProt 1–235

DNA-directed RNA polymerase subunit beta

Escherichia coli

UniProt P0A8V4

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 CCC; UniProt 1–1342 Not recorded 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 factor RpoS × 1 (A0A377K1M2) Synthetic DNA 50-mer (promoter non-template strand) × 1 Synthetic DNA 50-mer (promoter template strand) × 1 RNA 7-mer (de novo synthesized) × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 DPO DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;PEG3350, sodium chloride, HEPES Resolution 4.40 Å R-free 0.380

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.

113 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECO57
Isoform
PDB entities 2
Chains and sequence ranges Author chain CCC; 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 DDD; UniProt 1–1407 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoS × 1 (A0A377K1M2) Synthetic DNA 50-mer (promoter non-template strand) × 1 Synthetic DNA 50-mer (promoter template strand) × 1 RNA 7-mer (de novo synthesized) × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 DPO DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;PEG3350, sodium chloride, HEPES Resolution 4.40 Å R-free 0.380

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 DDD; 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 Other combination Heteromer Protein × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain EEE; UniProt 2–91 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma factor RpoS × 1 (A0A377K1M2) Synthetic DNA 50-mer (promoter non-template strand) × 1 Synthetic DNA 50-mer (promoter template strand) × 1 RNA 7-mer (de novo synthesized) × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 DPO DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;PEG3350, sodium chloride, HEPES Resolution 4.40 Å R-free 0.380

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 EEE; PDBConstruct 1–90; UniProt 2–91

RNA polymerase sigma factor RpoS

Escherichia coli

UniProt A0A377K1M2

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 FFF; UniProt 1–328 Mutation:I219G, S221A DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Synthetic DNA 50-mer (promoter non-template strand) × 1 Synthetic DNA 50-mer (promoter template strand) × 1 RNA 7-mer (de novo synthesized) × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 DPO DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295 K;PEG3350, sodium chloride, HEPES Resolution 4.40 Å R-free 0.380

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 A0A377K1M2_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain FFF; PDBConstruct 1–328; UniProt 1–328

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 6uu8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6uu8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6uu8
Deposition date deposition_date2019-10-30
Structure title titleE. coli mutant sigma-S transcription initiation complex with a 7-nt RNA ("Fresh" mutant crystal soaked with GTP, UTP, and CTP for 30 minutes)
Keywords keywords;Transcription initiation, RNA polymerase, DNA promoter, transcription bubble, de novo RNA synthesis, DNA scrunching, sigma-S factor, TRANSCRIPTION, TRANSFERASE-DNA-RNA complex ;; TRANSCRIPTION, TRANSFERASE/DNA/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.85
Radius of gyration Rg (electron density) rg_electron48.34
Forward intensity I(0) i02669850000.00
Molecular weight molecular_weight413210.0 kDa
Excluded volume excluded_volume510340 ų
Envelope volume envelope_volume736980 ų
Hydration-shell volume shell_volume119170 ų
Envelope diameter envelope_diameter165.7
Shell Rg shell_rg57.52
Envelope Rg envelope_rg48.29
Shape Rg shape_rg48.35
Total Rg total_rg48.59
Total atoms total_atoms28931
Residues n_residues3575
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 dmax157.7
Rg (real space) rg_real48.56
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.6700e+09
I(0) uncertainty (real space) i0_real_error5.0140e+07
Rg (reciprocal space) rg_reciprocal48.85
I(0) (reciprocal space) i0_reciprocal2671000000.0000
Solution quality estimate total_estimate0.6626
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.1
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha586500000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 0.087; Positv: 1.000; Valcen: 0.967; Smooth: 0.841

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)