7q4u

Cryo-EM structure of Mycobacterium tuberculosis RNA polymerase holoenzyme octamer comprising sigma factor SigB

Method: ELECTRON MICROSCOPY Dmax: 283.4 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis (strain ATCC 25618 / 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 heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain A; UniProt 1–347 Chain AA; UniProt 1–347 Chain B; UniProt 1–347 Chain FA; UniProt 1–347 Chain G; UniProt 1–347 Chain GA; UniProt 1–347 Chain H; UniProt 1–347 Chain LA; UniProt 1–347 Chain M; UniProt 1–347 Chain MA; UniProt 1–347 Chain N; UniProt 1–347 Chain RA; UniProt 1–347 Chain S; UniProt 1–347 Chain SA; UniProt 1–347 Chain T; UniProt 1–347 Chain Z; UniProt 1–347 Not recorded DNA-directed RNA polymerase subunit beta × 8 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 8 (P9WGY7) DNA-directed RNA polymerase subunit omega × 8 (P9WGY5) RNA polymerase sigma factor SigB × 8 (P9WGI5) ZN ZINC ION × 16 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 AA; PDBConstruct 1–347; UniProt 1–347 Author chain B; PDBConstruct 1–347; UniProt 1–347 Author chain FA; PDBConstruct 1–347; UniProt 1–347 Author chain G; PDBConstruct 1–347; UniProt 1–347 Author chain GA; PDBConstruct 1–347; UniProt 1–347 Author chain H; PDBConstruct 1–347; UniProt 1–347 Author chain LA; PDBConstruct 1–347; UniProt 1–347 Author chain M; PDBConstruct 1–347; UniProt 1–347 Author chain MA; PDBConstruct 1–347; UniProt 1–347 Author chain N; PDBConstruct 1–347; UniProt 1–347 Author chain RA; PDBConstruct 1–347; UniProt 1–347 Author chain S; PDBConstruct 1–347; UniProt 1–347 Author chain SA; PDBConstruct 1–347; UniProt 1–347 Author chain T; PDBConstruct 1–347; UniProt 1–347 Author chain Z; PDBConstruct 1–347; UniProt 1–347

DNA-directed RNA polymerase subunit beta

Mycobacterium tuberculosis (strain ATCC 25618 / 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 heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain BA; UniProt 6–1178 Chain C; UniProt 6–1178 Chain HA; UniProt 6–1178 Chain I; UniProt 6–1178 Chain NA; UniProt 6–1178 Chain O; UniProt 6–1178 Chain TA; UniProt 6–1178 Chain V; UniProt 6–1178 Mutation:L2E3G4C5 -> V DNA-directed RNA polymerase subunit alpha × 16 (P9WGZ1) ;DNA-directed RNA polymerase subunit beta' ; × 8 (P9WGY7) DNA-directed RNA polymerase subunit omega × 8 (P9WGY5) RNA polymerase sigma factor SigB × 8 (P9WGI5) ZN ZINC ION × 16 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 BA; PDBConstruct 2–1174; UniProt 6–1178 Author chain C; PDBConstruct 2–1174; UniProt 6–1178 Author chain HA; PDBConstruct 2–1174; UniProt 6–1178 Author chain I; PDBConstruct 2–1174; UniProt 6–1178 Author chain NA; PDBConstruct 2–1174; UniProt 6–1178 Author chain O; PDBConstruct 2–1174; UniProt 6–1178 Author chain TA; PDBConstruct 2–1174; UniProt 6–1178 Author chain V; PDBConstruct 2–1174; UniProt 6–1178

;DNA-directed RNA polymerase subunit beta' ;

Mycobacterium tuberculosis (strain ATCC 25618 / 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 heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain CA; UniProt 4–1316 Chain D; UniProt 4–1316 Chain IA; UniProt 4–1316 Chain J; UniProt 4–1316 Chain OA; UniProt 4–1316 Chain P; UniProt 4–1316 Chain UA; UniProt 4–1316 Chain W; UniProt 4–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 16 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 8 (P9WGY9) DNA-directed RNA polymerase subunit omega × 8 (P9WGY5) RNA polymerase sigma factor SigB × 8 (P9WGI5) ZN ZINC ION × 16 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 CA; PDBConstruct 1–1313; UniProt 4–1316 Author chain D; PDBConstruct 1–1313; UniProt 4–1316 Author chain IA; PDBConstruct 1–1313; UniProt 4–1316 Author chain J; PDBConstruct 1–1313; UniProt 4–1316 Author chain OA; PDBConstruct 1–1313; UniProt 4–1316 Author chain P; PDBConstruct 1–1313; UniProt 4–1316 Author chain UA; PDBConstruct 1–1313; UniProt 4–1316 Author chain W; PDBConstruct 1–1313; UniProt 4–1316

DNA-directed RNA polymerase subunit omega

Mycobacterium tuberculosis (strain ATCC 25618 / 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 heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain DA; UniProt 1–110 Chain E; UniProt 1–110 Chain JA; UniProt 1–110 Chain K; UniProt 1–110 Chain PA; UniProt 1–110 Chain Q; UniProt 1–110 Chain VA; UniProt 1–110 Chain X; UniProt 1–110 Not recorded DNA-directed RNA polymerase subunit alpha × 16 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 8 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 8 (P9WGY7) RNA polymerase sigma factor SigB × 8 (P9WGI5) ZN ZINC ION × 16 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 DA; PDBConstruct 1–110; UniProt 1–110 Author chain E; PDBConstruct 1–110; UniProt 1–110 Author chain JA; PDBConstruct 1–110; UniProt 1–110 Author chain K; PDBConstruct 1–110; UniProt 1–110 Author chain PA; PDBConstruct 1–110; UniProt 1–110 Author chain Q; PDBConstruct 1–110; UniProt 1–110 Author chain VA; PDBConstruct 1–110; UniProt 1–110 Author chain X; PDBConstruct 1–110; UniProt 1–110

RNA polymerase sigma factor SigB

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

UniProt P9WGI5

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain EA; UniProt 1–323 Chain F; UniProt 1–323 Chain KA; UniProt 1–323 Chain L; UniProt 1–323 Chain QA; UniProt 1–323 Chain R; UniProt 1–323 Chain WA; UniProt 1–323 Chain Y; UniProt 1–323 Not recorded DNA-directed RNA polymerase subunit alpha × 16 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 8 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 8 (P9WGY7) DNA-directed RNA polymerase subunit omega × 8 (P9WGY5) ZN ZINC ION × 16 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 SIGB_MYCTU
Isoform
PDB entities 5
Chains and sequence ranges Author chain EA; PDBConstruct 21–343; UniProt 1–323 Author chain F; PDBConstruct 21–343; UniProt 1–323 Author chain KA; PDBConstruct 21–343; UniProt 1–323 Author chain L; PDBConstruct 21–343; UniProt 1–323 Author chain QA; PDBConstruct 21–343; UniProt 1–323 Author chain R; PDBConstruct 21–343; UniProt 1–323 Author chain WA; PDBConstruct 21–343; UniProt 1–323 Author chain Y; PDBConstruct 21–343; UniProt 1–323

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 7q4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q4u
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7q4u
Deposition date deposition_date2021-11-02
Structure title titleCryo-EM structure of Mycobacterium tuberculosis RNA polymerase holoenzyme octamer comprising sigma factor SigB
Keywords keywordsDNA-dependent RNA polymerase, alternative sigma, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron113.50
Forward intensity I(0) i0102079000000.00
Molecular weight molecular_weight2709800.0 kDa
Excluded volume excluded_volume3385100 ų
Envelope volume envelope_volume6762700 ų
Hydration-shell volume shell_volume482130 ų
Envelope diameter envelope_diameter329.3
Shell Rg shell_rg121.50
Envelope Rg envelope_rg105.50
Shape Rg shape_rg113.50
Total Rg total_rg113.40
Total atoms total_atoms190528
Residues n_residues24472
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 dmax283.4
Rg (real space) rg_real112.20
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real9.7560e+10
I(0) uncertainty (real space) i0_real_error1.7180e+09
Rg (reciprocal space) rg_reciprocal122.10
I(0) (reciprocal space) i0_reciprocal105000000000.0000
Solution quality estimate total_estimate0.8547
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary161.9
Skewness Skewness skewness-0.146
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha1.9320
Highest regularization parameter α highest_alpha7066000000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.947; Sysdev: 1.000; Positv: 1.000; Valcen: 0.287; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)