6eec

Mycobacterium tuberculosis RNAP promoter unwinding intermediate complex with RbpA/CarD and AP3 promoter captured by Corallopyronin

Method: ELECTRON MICROSCOPY Dmax: 174.0 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis

UniProt A5U8D3

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 × 8 DNA 2 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 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (P9WGI0) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_MYCTA
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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–1172 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (P9WGI0) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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 A5U053

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 1–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (P9WGI0) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_MYCTA
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 3–1318; 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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain E; UniProt 41–149 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) RNA polymerase sigma factor SigA × 1 (P9WGI0) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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 P9WGI0

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 1–528 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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 SIGA_MYCTO
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 P9WHJ4

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain J; UniProt 1–111 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (P9WGI0) DNA (65-MER) × 1 DNA (63-MER) × 1 RNA polymerase-binding transcription factor CarD × 1 (P9WJG2) C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBPA_MYCTO
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–111; UniProt 1–111

RNA polymerase-binding transcription factor CarD

Mycobacterium tuberculosis

UniProt P9WJG2

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain M; UniProt 1–162 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A5U8D3) DNA-directed RNA polymerase subunit beta × 1 (V9Z879) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A5U053) DNA-directed RNA polymerase subunit omega × 1 (A0A0T9N9K3) RNA polymerase sigma factor SigA × 1 (P9WGI0) RNA polymerase-binding protein RbpA × 1 (P9WHJ4) DNA (65-MER) × 1 DNA (63-MER) × 1 C0L methyl [(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARD_MYCTO
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–162; UniProt 1–162

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 6eec

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6eec
Deposition date deposition_date2018-08-13
Structure title titleMycobacterium tuberculosis RNAP promoter unwinding intermediate complex with RbpA/CarD and AP3 promoter captured by Corallopyronin
Keywords keywordsinitiation, transcription bubble, closed clamp, open promoter complex, TRANSCRIPTION, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.01
Radius of gyration Rg (electron density) rg_electron50.89
Forward intensity I(0) i03011550000.00
Molecular weight molecular_weight427530.0 kDa
Excluded volume excluded_volume522620 ų
Envelope volume envelope_volume759440 ų
Hydration-shell volume shell_volume119590 ų
Envelope diameter envelope_diameter188.1
Shell Rg shell_rg57.60
Envelope Rg envelope_rg50.86
Shape Rg shape_rg50.87
Total Rg total_rg51.15
Total atoms total_atoms29936
Residues n_residues3636
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 dmax174.0
Rg (real space) rg_real51.90
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real3.0120e+09
I(0) uncertainty (real space) i0_real_error5.4780e+07
Rg (reciprocal space) rg_reciprocal52.10
I(0) (reciprocal space) i0_reciprocal3012000000.0000
Solution quality estimate total_estimate0.8639
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.8
Skewness Skewness skewness0.311
Kurtosis Kurtosis kurtosis-0.209
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha438600000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6eecA01
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_id6eecA02
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_id6eecB01
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_id6eecB02
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_id6eecC01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1110 — Dna-directed Rna Polymerase Ii 140kd Polypeptide; Chain: B; domain 3
Homologous superfamily homologous superfamily10 — RNA polymerase Rpb2, domain 2
Domain ID domain_id6eecD01
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_id6eecD02
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
Domain ID domain_id6eecM02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1290 — CarD-like, C-terminal domain

8. Citations (1)

9. Files and Curves (10)