6c06

Mycobacterium tuberculosis RNAP Holo/RbpA/Fidaxomicin

Method: ELECTRON MICROSCOPY Dmax: 183.5 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis

UniProt A0A045J8T1

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–347 Chain B; UniProt 1–347 Not recorded DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A045J9E2) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (A0A045HD00) RNA polymerase-binding protein RbpA × 1 (A0A045IP01) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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 A0A045J8T1_MYCTX
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 V9Z879

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–1172 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A045J8T1) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A045J9E2) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (A0A045HD00) RNA polymerase-binding protein RbpA × 1 (A0A045IP01) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V9Z879_MYCTX
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1172; UniProt 1–1172

;DNA-directed RNA polymerase subunit beta' ;

Mycobacterium tuberculosis

UniProt A0A045J9E2

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A045J8T1) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (A0A045HD00) RNA polymerase-binding protein RbpA × 1 (A0A045IP01) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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 A0A045J9E2_MYCTX
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

UniProt A0A0T9N9K3

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 41–149 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A045J8T1) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A045J9E2) RNA polymerase sigma factor SigA × 1 (A0A045HD00) RNA polymerase-binding protein RbpA × 1 (A0A045IP01) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0T9N9K3_MYCTX
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 2–110; UniProt 41–149

RNA polymerase sigma factor SigA

Mycobacterium tuberculosis

UniProt A0A045HD00

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 1–528 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A045J8T1) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A045J9E2) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase-binding protein RbpA × 1 (A0A045IP01) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A045HD00_MYCTX
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 4–531; UniProt 1–528

RNA polymerase-binding protein RbpA

Mycobacterium tuberculosis

UniProt A0A045IP01

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain J; UniProt 1–111 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A045J8T1) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A045J9E2) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (A0A045HD00) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 FI8 Fidaxomicin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.15 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 A0A045IP01_MYCTX
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–111; UniProt 1–111

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 6c06

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c06
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c06
Deposition date deposition_date2017-12-27
Structure title titleMycobacterium tuberculosis RNAP Holo/RbpA/Fidaxomicin
Keywords keywordsinitiation, antibiotic, switch region inhibitor, TRANSCRIPTION, transcription-antibiotic complex; transcription/antibiotic
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.37
Radius of gyration Rg (electron density) rg_electron50.92
Forward intensity I(0) i02020660000.00
Molecular weight molecular_weight371190.0 kDa
Excluded volume excluded_volume463700 ų
Envelope volume envelope_volume665640 ų
Hydration-shell volume shell_volume107870 ų
Envelope diameter envelope_diameter198.1
Shell Rg shell_rg56.18
Envelope Rg envelope_rg49.95
Shape Rg shape_rg50.93
Total Rg total_rg51.06
Total atoms total_atoms26170
Residues n_residues3353
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 dmax183.5
Rg (real space) rg_real51.31
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real2.0210e+09
I(0) uncertainty (real space) i0_real_error3.5080e+07
Rg (reciprocal space) rg_reciprocal51.41
I(0) (reciprocal space) i0_reciprocal2021000000.0000
Solution quality estimate total_estimate0.7662
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.1
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis0.109
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha265000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.652; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (2)

9. Files and Curves (10)