9e87

De Novo Mycobacterium tuberculosis transcription initiation pre-RPO promoter complex with open Beta' clamp (RNA Polymerase with Sigma-A, CarD, and RbpA)

Method: ELECTRON MICROSCOPY Dmax: 189.2 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis

UniProt A5U8D3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–347 Chain B; UniProt 1–347 Not recorded DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_MYCTA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–347; UniProt 1–347 Author chain B; PDBConstruct 1–347; UniProt 1–347

DNA-directed RNA polymerase subunit beta

Mycobacterium tuberculosis

UniProt A5U052

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–1177 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_MYCTA
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1177; UniProt 1–1177

;DNA-directed RNA polymerase subunit beta' ;

Mycobacterium tuberculosis

UniProt P0A675

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 1–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 RPOC_MYCBO
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 10–1325; UniProt 1–1316

DNA-directed RNA polymerase subunit omega

Mycobacterium tuberculosis

UniProt A0A045H2R3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain E; UniProt 1–110 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A045H2R3_MYCTX
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–110; UniProt 1–110

RNA polymerase sigma factor SigA

Mycobacterium tuberculosis

UniProt P0A603

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 1–528 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 SIGA_MYCBO
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 23–550; UniProt 1–528

RNA polymerase-binding protein RbpA

Mycobacterium tuberculosis

UniProt P9WHJ4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain J; UniProt 1–111 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD × 1 (Q12306,P9WJG2) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

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

View Construct and Data Evidence
UniProt name RBPA_MYCTO
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–111; UniProt 1–111

Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD

Mycobacterium tuberculosis

UniProt P9WJG2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain M; UniProt 1–162 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARD_MYCTO
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 124–285; UniProt 1–162

Ubiquitin-like protein SMT3,RNA polymerase-binding transcription factor CarD

Mycobacterium tuberculosis

UniProt Q12306

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain M; UniProt 1–98 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (A5U052) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A675) DNA-directed RNA polymerase subunit omega × 1 (A0A045H2R3) RNA polymerase sigma factor SigA × 1 (P0A603) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (62-MER) × 1 DNA (54-MER) × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

95 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMT3_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 25–122; UniProt 1–98

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 9e87

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e87
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e87
Deposition date deposition_date2024-11-05
Structure title titleDe Novo Mycobacterium tuberculosis transcription initiation pre-RPO promoter complex with open Beta' clamp (RNA Polymerase with Sigma-A, CarD, and RbpA)
Keywords keywordsPromoter escape, transcription, De novo, RNA polymerase, 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_guinier53.50
Radius of gyration Rg (electron density) rg_electron52.12
Forward intensity I(0) i02884240000.00
Molecular weight molecular_weight421300.0 kDa
Excluded volume excluded_volume516330 ų
Envelope volume envelope_volume780790 ų
Hydration-shell volume shell_volume120970 ų
Envelope diameter envelope_diameter202.4
Shell Rg shell_rg58.11
Envelope Rg envelope_rg51.94
Shape Rg shape_rg52.08
Total Rg total_rg52.40
Total atoms total_atoms57974
Residues n_residues3606
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 dmax189.2
Rg (real space) rg_real53.38
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real2.8840e+09
I(0) uncertainty (real space) i0_real_error6.3190e+07
Rg (reciprocal space) rg_reciprocal53.59
I(0) (reciprocal space) i0_reciprocal2885000000.0000
Solution quality estimate total_estimate0.8493
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.2
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.141
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha337100000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)