9m9e

Structural Basis of Pausing During Transcription Initiation in Mycobacterium tuberculosis

Method: ELECTRON MICROSCOPY Dmax: 180.2 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 Other combination Heteromer Protein × 7 DNA 2 RNA 1 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 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) ECF RNA polymerase sigma factor SigE × 1 (P9WGG7) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 Other combination Heteromer Protein × 7 DNA 2 RNA 1 PDB declaration: decameric(10) 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) ECF RNA polymerase sigma factor SigE × 1 (P9WGG7) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 Other combination Heteromer Protein × 7 DNA 2 RNA 1 PDB declaration: decameric(10) 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) ECF RNA polymerase sigma factor SigE × 1 (P9WGG7) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 Other combination Heteromer Protein × 7 DNA 2 RNA 1 PDB declaration: decameric(10) 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) ECF RNA polymerase sigma factor SigE × 1 (P9WGG7) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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

ECF RNA polymerase sigma factor SigE

Mycobacterium tuberculosis H37Rv

UniProt P9WGG7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 DNA 2 RNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 2–257 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) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG3) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIGE_MYCTU
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 8–263; UniProt 2–257

RNA polymerase-binding transcription factor CarD

Mycobacterium tuberculosis H37Rv

UniProt P9WJG3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 DNA 2 RNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain M; UniProt 2–162 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) ECF RNA polymerase sigma factor SigE × 1 (P9WGG7) DNA (48-MER) × 1 DNA (48-MER) × 1 ;RNA (5'-R(*CP*CP*CP*UP*CP*GP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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 CARD_MYCTU
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 9–169; UniProt 2–162

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 9m9e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m9e
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9m9e
Deposition date deposition_date2025-03-13
Structure title titleStructural Basis of Pausing During Transcription Initiation in Mycobacterium tuberculosis
Keywords keywords;RNA polymerase, Initiation complex, Pausing, Mycobacterium tuberculosis, Cryo-EM, TRANSCRIPTION/DNA/RNA, TRANSCRIPTION-DNA-RNA complex ;; TRANSCRIPTION/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.70
Radius of gyration Rg (electron density) rg_electron50.20
Forward intensity I(0) i02407630000.00
Molecular weight molecular_weight384490.0 kDa
Excluded volume excluded_volume471350 ų
Envelope volume envelope_volume710640 ų
Hydration-shell volume shell_volume114260 ų
Envelope diameter envelope_diameter195.2
Shell Rg shell_rg56.56
Envelope Rg envelope_rg50.07
Shape Rg shape_rg50.20
Total Rg total_rg50.37
Total atoms total_atoms26920
Residues n_residues3341
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 dmax180.2
Rg (real space) rg_real50.65
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real2.4080e+09
I(0) uncertainty (real space) i0_real_error4.7580e+07
Rg (reciprocal space) rg_reciprocal50.73
I(0) (reciprocal space) i0_reciprocal2408000000.0000
Solution quality estimate total_estimate0.8420
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.9
Skewness Skewness skewness0.408
Kurtosis Kurtosis kurtosis-0.014
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha493400000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.674; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)