7ckq

The cryo-EM structure of B. subtilis BmrR transcription activation complex

Method: ELECTRON MICROSCOPY Dmax: 186.8 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–314 Chain B; 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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–1193 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 1–1199 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain E; UniProt 1–67 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain F; UniProt 1–371 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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

Multidrug-efflux transporter 1 regulator

Bacillus subtilis (strain 168)

UniProt P39075

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain G; UniProt 1–278 Chain I; UniProt 1–278 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 UPF0356 protein YkzG × 1 (O31718) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMRR_BACSU
Isoform
PDB entities 8
Chains and sequence ranges Author chain G; PDBConstruct 5–282; UniProt 1–278 Author chain I; PDBConstruct 5–282; UniProt 1–278

UPF0356 protein YkzG

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain H; UniProt 1–69 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (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 (50-MER) × 1 DNA (50-MER) × 1 Multidrug-efflux transporter 1 regulator × 2 (P39075) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 P4P TETRAPHENYLPHOSPHONIUM × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 YKZG_BACSU
Isoform
PDB entities 9
Chains and sequence ranges Author chain H; PDBConstruct 1–69; UniProt 1–69

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 7ckq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7ckq
Deposition date deposition_date2020-07-18
Structure title titleThe cryo-EM structure of B. subtilis BmrR transcription activation complex
Keywords keywordsRNA polymerase, Transcription activation, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.29
Radius of gyration Rg (electron density) rg_electron52.50
Forward intensity I(0) i02445050000.00
Molecular weight molecular_weight390890.0 kDa
Excluded volume excluded_volume479420 ų
Envelope volume envelope_volume733500 ų
Hydration-shell volume shell_volume114640 ų
Envelope diameter envelope_diameter205.6
Shell Rg shell_rg57.18
Envelope Rg envelope_rg52.23
Shape Rg shape_rg52.53
Total Rg total_rg52.57
Total atoms total_atoms27484
Residues n_residues3675
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 dmax186.8
Rg (real space) rg_real52.28
Rg uncertainty (real space) rg_real_error1.87
I(0) (real space) i0_real2.4450e+09
I(0) uncertainty (real space) i0_real_error4.9600e+07
Rg (reciprocal space) rg_reciprocal52.28
I(0) (reciprocal space) i0_reciprocal2445000000.0000
Solution quality estimate total_estimate0.8511
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.2
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.127
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha393600000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)