8xa6

Cryo-EM structure of Bacillus RNAP and SPO1 gp33 complex

Method: ELECTRON MICROSCOPY Dmax: 155.6 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count 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) DNA-directed RNA polymerase subunit delta × 1 (P12464) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count 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) DNA-directed RNA polymerase subunit delta × 1 (P12464) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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' ;

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count 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) DNA-directed RNA polymerase subunit delta × 1 (P12464) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; 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) DNA-directed RNA polymerase subunit delta × 1 (P12464) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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 F; PDBConstruct 1–67; UniProt 1–67

DNA-directed RNA polymerase subunit delta

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain L; UniProt 1–173 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-directed RNA polymerase subunit epsilon × 1 (O31718) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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 5
Chains and sequence ranges Author chain L; PDBConstruct 1–173; UniProt 1–173

DNA-directed RNA polymerase subunit epsilon

Bacillus

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–69 Mutation:V33I 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-directed RNA polymerase subunit delta × 1 (P12464) Gene 33 protein × 1 (P06226) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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 E; PDBConstruct 1–69; UniProt 1–69

Gene 33 protein

Bacillus phage SPO1

UniProt P06226

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain H; UniProt 1–101 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-directed RNA polymerase subunit delta × 1 (P12464) DNA-directed RNA polymerase subunit epsilon × 1 (O31718) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.02 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 GP33_BPSP1
Isoform
PDB entities 7
Chains and sequence ranges Author chain H; PDBConstruct 1–101; UniProt 1–101

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 8xa6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xa6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xa6
Deposition date deposition_date2023-12-02
Structure title titleCryo-EM structure of Bacillus RNAP and SPO1 gp33 complex
Keywords keywordsbacterial, phage, complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.23
Radius of gyration Rg (electron density) rg_electron47.66
Forward intensity I(0) i01710920000.00
Molecular weight molecular_weight345040.0 kDa
Excluded volume excluded_volume432940 ų
Envelope volume envelope_volume688840 ų
Hydration-shell volume shell_volume113190 ų
Envelope diameter envelope_diameter168.6
Shell Rg shell_rg56.69
Envelope Rg envelope_rg47.43
Shape Rg shape_rg47.68
Total Rg total_rg47.92
Total atoms total_atoms48778
Residues n_residues3079
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 dmax155.6
Rg (real space) rg_real47.94
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real1.7110e+09
I(0) uncertainty (real space) i0_real_error3.0820e+07
Rg (reciprocal space) rg_reciprocal48.23
I(0) (reciprocal space) i0_reciprocal1712000000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.202
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha788400000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)