6bzo

Mtb RNAP Holo/RbpA/Fidaxomicin/upstream fork DNA

Method: ELECTRON MICROSCOPY Dmax: 181.3 Å Quality: REASONABLE

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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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–DNA Heteromer Protein × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts 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) DNA (32-MER) × 1 DNA (26-MER) × 1 FI8 Fidaxomicin × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 6bzo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6bzo
Deposition date deposition_date2017-12-25
Structure title titleMtb RNAP Holo/RbpA/Fidaxomicin/upstream fork DNA
Keywords keywordsRNA Polymerase, Antibiotic, Inhibitor, TRANSCRIPTION, transcription-dna-antibiotic complex; transcription/dna/antibiotic
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.15
Radius of gyration Rg (electron density) rg_electron51.19
Forward intensity I(0) i02341020000.00
Molecular weight molecular_weight388690.0 kDa
Excluded volume excluded_volume480720 ų
Envelope volume envelope_volume720950 ų
Hydration-shell volume shell_volume114250 ų
Envelope diameter envelope_diameter197.7
Shell Rg shell_rg57.38
Envelope Rg envelope_rg50.57
Shape Rg shape_rg51.17
Total Rg total_rg51.42
Total atoms total_atoms27330
Residues n_residues3410
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 dmax181.3
Rg (real space) rg_real52.05
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real2.3410e+09
I(0) uncertainty (real space) i0_real_error4.6330e+07
Rg (reciprocal space) rg_reciprocal52.23
I(0) (reciprocal space) i0_reciprocal2342000000.0000
Solution quality estimate total_estimate0.6247
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.080
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha290200000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 1.000; Sysdev: 0.007; Positv: 1.000; Valcen: 0.970; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6bzoA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id6bzoA02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology120 — RNA Polymerase Alpha Subunit; Chain A, domain 2
Homologous superfamily homologous superfamily12 — DNA-directed RNA polymerase, insert domain
Domain ID domain_id6bzoB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id6bzoB02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology120 — RNA Polymerase Alpha Subunit; Chain A, domain 2
Homologous superfamily homologous superfamily12 — DNA-directed RNA polymerase, insert domain
Domain ID domain_id6bzoD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily100 — RNA polymerase Rpb1, domain 3
Domain ID domain_id6bzoD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily30 — RNA polymerase Rpb1 funnel domain

8. Citations (1)

9. Files and Curves (10)