6wmu

E. coli RNAPs70-SspA-gadA DNA complex

Method: ELECTRON MICROSCOPY Dmax: 174.4 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt A0A073G207

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 × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–329 Chain B; UniProt 1–329 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 (P0A802) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 Stringent starvation protein A × 2 (A0A1X3LEF3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A073G207_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–329; UniProt 1–329 Author chain B; PDBConstruct 1–329; UniProt 1–329

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 Protein–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 1–1342 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A073G207) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A802) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 Stringent starvation protein A × 2 (A0A1X3LEF3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

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 C; 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 × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–1407 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A073G207) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) DNA-directed RNA polymerase subunit omega × 1 (P0A802) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 Stringent starvation protein A × 2 (A0A1X3LEF3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1407; UniProt 1–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli

UniProt P0A802

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 × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A073G207) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 Stringent starvation protein A × 2 (A0A1X3LEF3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECO57
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 1–91

RNA polymerase sigma factor RpoD

Escherichia coli

UniProt Q0P6L9

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 × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 1–613 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A073G207) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 Stringent starvation protein A × 2 (A0A1X3LEF3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

32 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q0P6L9_ECOLX
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–613; UniProt 1–613

Stringent starvation protein A

Escherichia coli TA054

UniProt A0A1X3LEF3

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 × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–212 Chain L; UniProt 1–212 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A073G207) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A802) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA NT-strand × 1 DNA T-strand × 1 DNA NT-strand downstream × 1 DNA T-strand downstream × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A1X3LEF3_ECOLX
Isoform
PDB entities 10
Chains and sequence ranges Author chain K; PDBConstruct 21–232; UniProt 1–212 Author chain L; PDBConstruct 21–232; UniProt 1–212

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 6wmu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6wmu
Deposition date deposition_date2020-04-21
Structure title titleE. coli RNAPs70-SspA-gadA DNA complex
Keywords keywordsRNA polymerase complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.67
Radius of gyration Rg (electron density) rg_electron53.22
Forward intensity I(0) i03659310000.00
Molecular weight molecular_weight486960.0 kDa
Excluded volume excluded_volume601690 ų
Envelope volume envelope_volume873100 ų
Hydration-shell volume shell_volume131290 ų
Envelope diameter envelope_diameter183.7
Shell Rg shell_rg60.20
Envelope Rg envelope_rg52.53
Shape Rg shape_rg53.23
Total Rg total_rg53.37
Total atoms total_atoms34094
Residues n_residues4207
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 dmax174.4
Rg (real space) rg_real53.47
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.6590e+09
I(0) uncertainty (real space) i0_real_error6.5510e+07
Rg (reciprocal space) rg_reciprocal53.83
I(0) (reciprocal space) i0_reciprocal3661000000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.2
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.379
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha528500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6wmuC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily150 — RNA polymerase II, Rpb2 subunit, wall domain
Domain ID domain_id6wmuD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily30 — RNA polymerase Rpb1 funnel domain
Domain ID domain_id6wmuD02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain

8. Citations (1)

9. Files and Curves (10)