7xug

cryo-EM structure of HK022 putRNA-less E.coli RNA polymerase elongation complex

Method: ELECTRON MICROSCOPY Dmax: 156.4 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli (strain K12)

UniProt P0A7Z4

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 G; UniProt 1–329 Chain H; UniProt 1–329 Not recorded non-template DNA × 1 template DNA × 1 RNA (nun gene and immunity region) × 1 DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;pH adjustment at 4'C cryo-EM vitrification conditions:Cryogen ETHANE;using two layers of blot papers Resolution 3.57 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.

276 other PDB entries and 305 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–329; UniProt 1–329 Author chain H; PDBConstruct 1–329; UniProt 1–329

DNA-directed RNA polymerase subunit beta

Escherichia coli (strain K12)

UniProt P0A8V2

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 I; UniProt 1–1342 Not recorded non-template DNA × 1 template DNA × 1 RNA (nun gene and immunity region) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;pH adjustment at 4'C cryo-EM vitrification conditions:Cryogen ETHANE;using two layers of blot papers Resolution 3.57 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.

219 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli (strain K12)

UniProt P0A8T7

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 J; UniProt 1–1407 Not recorded non-template DNA × 1 template DNA × 1 RNA (nun gene and immunity region) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;pH adjustment at 4'C cryo-EM vitrification conditions:Cryogen ETHANE;using two layers of blot papers Resolution 3.57 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.

239 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–1407; UniProt 1–1407

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 K; UniProt 1–91 Not recorded non-template DNA × 1 template DNA × 1 RNA (nun gene and immunity region) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;pH adjustment at 4'C cryo-EM vitrification conditions:Cryogen ETHANE;using two layers of blot papers Resolution 3.57 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 7
Chains and sequence ranges Author chain K; 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 7xug

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xug
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7xug
Deposition date deposition_date2022-05-18
Structure title titlecryo-EM structure of HK022 putRNA-less E.coli RNA polymerase elongation complex
Keywords keywordsbacterial transcription, HK022 put, anti-termination, anti-pausing, cryo-EM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.12
Radius of gyration Rg (electron density) rg_electron47.87
Forward intensity I(0) i02155910000.00
Molecular weight molecular_weight371710.0 kDa
Excluded volume excluded_volume459610 ų
Envelope volume envelope_volume672170 ų
Hydration-shell volume shell_volume111000 ų
Envelope diameter envelope_diameter168.9
Shell Rg shell_rg56.14
Envelope Rg envelope_rg47.73
Shape Rg shape_rg47.89
Total Rg total_rg48.10
Total atoms total_atoms26026
Residues n_residues3232
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 dmax156.4
Rg (real space) rg_real47.89
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real2.1560e+09
I(0) uncertainty (real space) i0_real_error3.7860e+07
Rg (reciprocal space) rg_reciprocal48.12
I(0) (reciprocal space) i0_reciprocal2157000000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.9
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha472600000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.864

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7xugG01
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_id7xugH01
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_id7xugJ01
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_id7xugJ02
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

8. Citations (1)

9. Files and Curves (10)