7mko

Escherichia coli RNA polymerase elongation complex

Method: ELECTRON MICROSCOPY Dmax: 150.6 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli (strain K12)

UniProt A0A4S5AL01

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–237 Chain B; UniProt 1–237 Not recorded DNA-directed RNA polymerase subunit beta × 1 (A0A4S4NK82) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A6D2WUT6) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (29-MER) × 1 RNA (20-MER) × 1 DNA (29-MER) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 2TM 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]cytidine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.15 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.

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

View Construct and Data Evidence
UniProt name A0A4S5AL01_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–237; UniProt 1–237 Author chain B; PDBConstruct 1–237; UniProt 1–237

DNA-directed RNA polymerase subunit beta

Escherichia coli (strain K12)

UniProt A0A4S4NK82

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain C; UniProt 3–1342 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A4S5AL01) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A6D2WUT6) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (29-MER) × 1 RNA (20-MER) × 1 DNA (29-MER) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 2TM 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]cytidine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.15 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 A0A4S4NK82_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1340; UniProt 3–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli (strain K12)

UniProt A0A6D2WUT6

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain D; UniProt 14–1376 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A4S5AL01) DNA-directed RNA polymerase subunit beta × 1 (A0A4S4NK82) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA (29-MER) × 1 RNA (20-MER) × 1 DNA (29-MER) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 2TM 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]cytidine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.15 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 A0A6D2WUT6_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1363; UniProt 14–1376

DNA-directed RNA polymerase subunit omega

Escherichia coli (strain K12)

UniProt P0A800

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (A0A4S5AL01) DNA-directed RNA polymerase subunit beta × 1 (A0A4S4NK82) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A6D2WUT6) DNA (29-MER) × 1 RNA (20-MER) × 1 DNA (29-MER) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 2TM 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]cytidine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.15 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.

258 other PDB entries and 277 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 1–91

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 7mko

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mko
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mko
Deposition date deposition_date2021-04-26
Structure title titleEscherichia coli RNA polymerase elongation complex
Keywords keywordsRNAP recycling, RapA, Post-Termination Complex, PTC, TRANSCRIPTION, TRANSCRIPTION-DNA-RNA complex; TRANSCRIPTION/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.11
Radius of gyration Rg (electron density) rg_electron46.93
Forward intensity I(0) i02211900000.00
Molecular weight molecular_weight375250.0 kDa
Excluded volume excluded_volume463430 ų
Envelope volume envelope_volume652150 ų
Hydration-shell volume shell_volume109280 ų
Envelope diameter envelope_diameter160.5
Shell Rg shell_rg55.43
Envelope Rg envelope_rg47.06
Shape Rg shape_rg46.95
Total Rg total_rg47.14
Total atoms total_atoms26269
Residues n_residues3256
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 dmax150.6
Rg (real space) rg_real46.91
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.2120e+09
I(0) uncertainty (real space) i0_real_error3.8140e+07
Rg (reciprocal space) rg_reciprocal47.11
I(0) (reciprocal space) i0_reciprocal2212000000.0000
Solution quality estimate total_estimate0.8727
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.3
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha531200000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.781

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id7mkoA01
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_id7mkoB01
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_id7mkoD01
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_id7mkoD02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id7mkoE01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology940 — Eukaryotic RPB6 RNA polymerase subunit
Homologous superfamily homologous superfamily10 — RNA polymerase subunit, RPB6/omega

8. Citations (1)

9. Files and Curves (10)