7f75

Cryo-EM structure of Spx-dependent transcription activation complex

Method: ELECTRON MICROSCOPY Dmax: 168.8 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

OrganismNot specified

UniProt P20429

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–314 Chain B; UniProt 1–314 Chain I; UniProt 1–314 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P37870) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) DNA-directed RNA polymerase subunit omega × 1 (O35011) RNA polymerase sigma factor SigA × 1 (P06224) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–314; UniProt 1–314 Author chain B; PDBConstruct 1–314; UniProt 1–314 Author chain I; PDBConstruct 1–314; UniProt 1–314

DNA-directed RNA polymerase subunit beta

OrganismNot specified

UniProt P37870

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 1–1193 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) DNA-directed RNA polymerase subunit omega × 1 (O35011) RNA polymerase sigma factor SigA × 1 (P06224) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_BACSU
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1193; UniProt 1–1193

;DNA-directed RNA polymerase subunit beta' ;

OrganismNot specified

UniProt P37871

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–1199 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) DNA-directed RNA polymerase subunit beta × 1 (P37870) DNA-directed RNA polymerase subunit omega × 1 (O35011) RNA polymerase sigma factor SigA × 1 (P06224) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 RPOC_BACSU
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1199; UniProt 1–1199

DNA-directed RNA polymerase subunit omega

OrganismNot specified

UniProt O35011

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–67 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) DNA-directed RNA polymerase subunit beta × 1 (P37870) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) RNA polymerase sigma factor SigA × 1 (P06224) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 RPOZ_BACSU
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–67; UniProt 1–67

RNA polymerase sigma factor SigA

OrganismNot specified

UniProt P06224

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 1–371 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) DNA-directed RNA polymerase subunit beta × 1 (P37870) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) DNA-directed RNA polymerase subunit omega × 1 (O35011) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIGA_BACSU
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–371; UniProt 1–371

DNA-directed RNA polymerase subunit epsilon

OrganismNot specified

UniProt O31718

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain H; UniProt 1–69 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) DNA-directed RNA polymerase subunit beta × 1 (P37870) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) DNA-directed RNA polymerase subunit omega × 1 (O35011) RNA polymerase sigma factor SigA × 1 (P06224) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 DNA-directed RNA polymerase subunit delta × 1 (P12464) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOY_BACSU
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–69; UniProt 1–69

DNA-directed RNA polymerase subunit delta

OrganismNot specified

UniProt P12464

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 1–173 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P20429) DNA-directed RNA polymerase subunit beta × 1 (P37870) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P37871) DNA-directed RNA polymerase subunit omega × 1 (O35011) RNA polymerase sigma factor SigA × 1 (P06224) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) transcriptional regulator Spx × 1 trxA promoter DNA-Non template strand × 1 trxA promoter DNA-template strand × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOE_BACSU
Isoform
PDB entities 10
Chains and sequence ranges Author chain L; PDBConstruct 1–173; UniProt 1–173

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 7f75

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7f75
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7f75
Deposition date deposition_date2021-06-28
Structure title titleCryo-EM structure of Spx-dependent transcription activation complex
Keywords keywordsComplex, transcription activator, stress, oxidated form, 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_guinier51.55
Radius of gyration Rg (electron density) rg_electron50.65
Forward intensity I(0) i02480090000.00
Molecular weight molecular_weight383360.0 kDa
Excluded volume excluded_volume465990 ų
Envelope volume envelope_volume731730 ų
Hydration-shell volume shell_volume116630 ų
Envelope diameter envelope_diameter180.4
Shell Rg shell_rg57.29
Envelope Rg envelope_rg49.74
Shape Rg shape_rg50.61
Total Rg total_rg50.96
Total atoms total_atoms26887
Residues n_residues3532
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 dmax168.8
Rg (real space) rg_real51.38
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real2.4800e+09
I(0) uncertainty (real space) i0_real_error4.4940e+07
Rg (reciprocal space) rg_reciprocal51.67
I(0) (reciprocal space) i0_reciprocal2481000000.0000
Solution quality estimate total_estimate0.8843
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.3
Skewness Skewness skewness0.210
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha471700000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)