6zfb

Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer)

Method: ELECTRON MICROSCOPY Dmax: 268.0 Å Quality: GOOD

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

RNA polymerase subunit omega

OrganismNot specified

UniProt A0A410WI33

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain E; UniProt 1–69 Chain e; UniProt 1–69 Not recorded DNA-directed RNA polymerase subunit delta × 2 DNA-directed RNA polymerase subunit alpha × 4 (A0A063XB83) DNA-directed RNA polymerase subunit beta × 2 (A0A2J0WBQ0) ;DNA-directed RNA polymerase subunit beta' ; × 2 (A0A063XB23) DNA helicase × 2 (A0A164TSE8) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A410WI33_BACVA
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–69; UniProt 1–69 Author chain e; PDBConstruct 1–69; UniProt 1–69

DNA-directed RNA polymerase subunit alpha

OrganismNot specified

UniProt A0A063XB83

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain U; UniProt 1–314 Chain V; UniProt 1–314 Chain u; UniProt 1–314 Chain v; UniProt 1–314 Not recorded DNA-directed RNA polymerase subunit delta × 2 RNA polymerase subunit omega × 2 (A0A410WI33) DNA-directed RNA polymerase subunit beta × 2 (A0A2J0WBQ0) ;DNA-directed RNA polymerase subunit beta' ; × 2 (A0A063XB23) DNA helicase × 2 (A0A164TSE8) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A063XB83_BACIU
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 1–314; UniProt 1–314 Author chain V; PDBConstruct 1–314; UniProt 1–314 Author chain u; PDBConstruct 1–314; UniProt 1–314 Author chain v; PDBConstruct 1–314; UniProt 1–314

DNA-directed RNA polymerase subunit beta

OrganismNot specified

UniProt A0A2J0WBQ0

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain X; UniProt 1–1193 Chain x; UniProt 1–1193 Not recorded DNA-directed RNA polymerase subunit delta × 2 RNA polymerase subunit omega × 2 (A0A410WI33) DNA-directed RNA polymerase subunit alpha × 4 (A0A063XB83) ;DNA-directed RNA polymerase subunit beta' ; × 2 (A0A063XB23) DNA helicase × 2 (A0A164TSE8) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2J0WBQ0_BACIU
Isoform
PDB entities 4
Chains and sequence ranges Author chain X; PDBConstruct 1–1193; UniProt 1–1193 Author chain x; PDBConstruct 1–1193; UniProt 1–1193

;DNA-directed RNA polymerase subunit beta' ;

OrganismNot specified

UniProt A0A063XB23

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain Y; UniProt 1–1199 Chain y; UniProt 1–1199 Not recorded DNA-directed RNA polymerase subunit delta × 2 RNA polymerase subunit omega × 2 (A0A410WI33) DNA-directed RNA polymerase subunit alpha × 4 (A0A063XB83) DNA-directed RNA polymerase subunit beta × 2 (A0A2J0WBQ0) DNA helicase × 2 (A0A164TSE8) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A063XB23_BACIU
Isoform
PDB entities 5
Chains and sequence ranges Author chain Y; PDBConstruct 1–1199; UniProt 1–1199 Author chain y; PDBConstruct 1–1199; UniProt 1–1199

DNA helicase

OrganismNot specified

UniProt A0A164TSE8

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain H; UniProt 1–774 Chain h; UniProt 1–774 Not recorded DNA-directed RNA polymerase subunit delta × 2 RNA polymerase subunit omega × 2 (A0A410WI33) DNA-directed RNA polymerase subunit alpha × 4 (A0A063XB83) DNA-directed RNA polymerase subunit beta × 2 (A0A2J0WBQ0) ;DNA-directed RNA polymerase subunit beta' ; × 2 (A0A063XB23) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A164TSE8_BACIU
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–774; UniProt 1–774 Author chain h; PDBConstruct 1–774; UniProt 1–774

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 6zfb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6zfb
Deposition date deposition_date2020-06-17
Structure title titleStructure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer)
Keywords keywordsTRANSCRIPTION/DNA/RNA, DNA-DEPENDENT RNA POLYMERASE, BACTERIAL, TRANSCRIPTION, Helicase; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier77.78
Radius of gyration Rg (electron density) rg_electron77.89
Forward intensity I(0) i09270080000.00
Molecular weight molecular_weight816990.0 kDa
Excluded volume excluded_volume1023100 ų
Envelope volume envelope_volume1644300 ų
Hydration-shell volume shell_volume177930 ų
Envelope diameter envelope_diameter267.6
Shell Rg shell_rg73.61
Envelope Rg envelope_rg75.29
Shape Rg shape_rg77.91
Total Rg total_rg77.77
Total atoms total_atoms57505
Residues n_residues7313
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 dmax268.0
Rg (real space) rg_real81.32
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real9.2740e+09
I(0) uncertainty (real space) i0_real_error1.8840e+08
Rg (reciprocal space) rg_reciprocal76.91
I(0) (reciprocal space) i0_reciprocal9248000000.0000
Solution quality estimate total_estimate0.8713
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.4
Skewness Skewness skewness0.475
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha1.4070
Highest regularization parameter α highest_alpha676400000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 0.873; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.137

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id6zfbH01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6zfbX01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily150 — RNA polymerase II, Rpb2 subunit, wall domain
Domain ID domain_id6zfbY01
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_id6zfbY02
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_id6zfbh01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6zfbu01
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_id6zfbx01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily150 — RNA polymerase II, Rpb2 subunit, wall domain
Domain ID domain_id6zfby01
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_id6zfby02
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)