8ej3

M. tuberculosis RNAP pause escaped complex with Bacillus subtilis NusG and GMPCPP

Method: ELECTRON MICROSCOPY Dmax: 181.3 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 × 6 DNA 2 RNA 1 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 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Transcription termination/antitermination protein NusG × 1 (Q06795) DNA (29-MER) × 1 ;RNA (5'-R(P*UP*CP*GP*GP*CP*AP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA (32-MER) × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 4-5 seconds before plunging in liquid ethane Resolution 3.13 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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) 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) Transcription termination/antitermination protein NusG × 1 (Q06795) DNA (29-MER) × 1 ;RNA (5'-R(P*UP*CP*GP*GP*CP*AP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA (32-MER) × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 4-5 seconds before plunging in liquid ethane Resolution 3.13 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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) 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) Transcription termination/antitermination protein NusG × 1 (Q06795) DNA (29-MER) × 1 ;RNA (5'-R(P*UP*CP*GP*GP*CP*AP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA (32-MER) × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 4-5 seconds before plunging in liquid ethane Resolution 3.13 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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) 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) Transcription termination/antitermination protein NusG × 1 (Q06795) DNA (29-MER) × 1 ;RNA (5'-R(P*UP*CP*GP*GP*CP*AP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA (32-MER) × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 4-5 seconds before plunging in liquid ethane Resolution 3.13 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

Transcription termination/antitermination protein NusG

Bacillus subtilis subsp. subtilis str. 168

UniProt Q06795

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain G; UniProt 1–177 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 (29-MER) × 1 ;RNA (5'-R(P*UP*CP*GP*GP*CP*AP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA (32-MER) × 1 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 4-5 seconds before plunging in liquid ethane Resolution 3.13 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUSG_BACSU
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–177; UniProt 1–177

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 8ej3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ej3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ej3
Deposition date deposition_date2022-09-16
Structure title titleM. tuberculosis RNAP pause escaped complex with Bacillus subtilis NusG and GMPCPP
Keywords keywordsTranscription elongation RNA polymerase pausing NusG cryo-EM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.16
Radius of gyration Rg (electron density) rg_electron48.05
Forward intensity I(0) i02112910000.00
Molecular weight molecular_weight361830.0 kDa
Excluded volume excluded_volume444710 ų
Envelope volume envelope_volume665210 ų
Hydration-shell volume shell_volume110700 ų
Envelope diameter envelope_diameter195.0
Shell Rg shell_rg55.65
Envelope Rg envelope_rg47.90
Shape Rg shape_rg48.08
Total Rg total_rg48.22
Total atoms total_atoms25330
Residues n_residues3136
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_real48.11
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real2.1130e+09
I(0) uncertainty (real space) i0_real_error3.8130e+07
Rg (reciprocal space) rg_reciprocal48.16
I(0) (reciprocal space) i0_reciprocal2113000000.0000
Solution quality estimate total_estimate0.8097
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.4
Skewness Skewness skewness0.457
Kurtosis Kurtosis kurtosis0.217
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha771800000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.517; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8ej3B01
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_id8ej3D01
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_id8ej3D02
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)