9keu

Cryo-EM structure of Mycobacterium tuberculosis transcription activation complex with four PhoP molecules (composite map)

Method: ELECTRON MICROSCOPY Dmax: 205.3 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis H37Rv

UniProt P9WGZ1

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: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 1–347 Chain B; UniProt 1–347 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 RNA polymerase sigma factor SigA × 1 (P9WGI1) Possible two component system response transcriptional positive regulator PhoP × 4 (P71814) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

50 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_MYCTU
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 H37Rv

UniProt P9WGY9

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: 12-meric(12) Consistent with all polymer counts Chain C; UniProt 1–1178 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P9WGZ1) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 RNA polymerase sigma factor SigA × 1 (P9WGI1) Possible two component system response transcriptional positive regulator PhoP × 4 (P71814) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

53 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_MYCTU
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1178; UniProt 1–1178

;DNA-directed RNA polymerase subunit beta' ;

Mycobacterium tuberculosis H37Rv

UniProt P9WGY7

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: 12-meric(12) Consistent with all polymer counts Chain D; UniProt 1–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 RNA polymerase sigma factor SigA × 1 (P9WGI1) Possible two component system response transcriptional positive regulator PhoP × 4 (P71814) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

51 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_MYCTU
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1316; UniProt 1–1316

DNA-directed RNA polymerase subunit omega

Mycobacterium tuberculosis H37Rv

UniProt P9WGY5

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: 12-meric(12) Consistent with all polymer counts Chain E; UniProt 1–110 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 RNA polymerase sigma factor SigA × 1 (P9WGI1) Possible two component system response transcriptional positive regulator PhoP × 4 (P71814) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

46 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

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

RNA polymerase sigma factor SigA

Mycobacterium tuberculosis H37Rv

UniProt P9WGI1

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: 12-meric(12) Consistent with all polymer counts Chain F; UniProt 1–528 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 Possible two component system response transcriptional positive regulator PhoP × 4 (P71814) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIGA_MYCTU
Isoform
PDB entities 7
Chains and sequence ranges Author chain F; PDBConstruct 1–528; UniProt 1–528

Possible two component system response transcriptional positive regulator PhoP

Mycobacterium tuberculosis H37Rv

UniProt P71814

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: 12-meric(12) Consistent with all polymer counts Chain I; UniProt 1–247 Chain J; UniProt 1–247 Chain K; UniProt 1–247 Chain M; UniProt 1–247 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of the promoter × 1 Template strand DNA of the promoter × 1 RNA polymerase sigma factor SigA × 1 (P9WGI1) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 P71814_MYCTU
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–247; UniProt 1–247 Author chain J; PDBConstruct 1–247; UniProt 1–247 Author chain K; PDBConstruct 1–247; UniProt 1–247 Author chain M; PDBConstruct 1–247; UniProt 1–247

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 9keu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9keu
Deposition date deposition_date2024-11-05
Structure title titleCryo-EM structure of Mycobacterium tuberculosis transcription activation complex with four PhoP molecules (composite map)
Keywords keywordsbacterial RNA polymerase, GENE REGULATION-DNA COMPLEX; GENE REGULATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.10
Radius of gyration Rg (electron density) rg_electron55.91
Forward intensity I(0) i03352700000.00
Molecular weight molecular_weight449880.0 kDa
Excluded volume excluded_volume548790 ų
Envelope volume envelope_volume847430 ų
Hydration-shell volume shell_volume124720 ų
Envelope diameter envelope_diameter220.7
Shell Rg shell_rg59.50
Envelope Rg envelope_rg56.48
Shape Rg shape_rg55.88
Total Rg total_rg56.08
Total atoms total_atoms31457
Residues n_residues3796
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 dmax205.3
Rg (real space) rg_real57.19
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real3.3530e+09
I(0) uncertainty (real space) i0_real_error6.3170e+07
Rg (reciprocal space) rg_reciprocal57.01
I(0) (reciprocal space) i0_reciprocal3352000000.0000
Solution quality estimate total_estimate0.8543
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.172
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha507900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.724; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)