7d7c

CryoEM structure of gp55-dependent RNA polymerase-promoter open complex

Method: ELECTRON MICROSCOPY Dmax: 157.2 Å Quality: REASONABLE

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt U9ZUN7

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–329 Chain B; UniProt 1–329 Not recorded DNA-directed RNA polymerase subunit beta × 1 (A0A080FHH4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (D7Y6A2) DNA (template strand) × 1 gp55 × 1 DNA (nontemplate strand) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 U9ZUN7_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–329; UniProt 1–329 Author chain B; PDBConstruct 1–329; UniProt 1–329

DNA-directed RNA polymerase subunit beta

Escherichia coli 1-392-07_S4_C3

UniProt A0A080FHH4

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain C; UniProt 1–1342 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (U9ZUN7) ;DNA-directed RNA polymerase subunit beta' ; × 1 (D7Y6A2) DNA (template strand) × 1 gp55 × 1 DNA (nontemplate strand) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 A0A080FHH4_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

UniProt D7Y6A2

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain D; UniProt 1–1407 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (U9ZUN7) DNA-directed RNA polymerase subunit beta × 1 (A0A080FHH4) DNA (template strand) × 1 gp55 × 1 DNA (nontemplate strand) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 D7Y6A2_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1407; UniProt 1–1407

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 7d7c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d7c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d7c
Deposition date deposition_date2020-10-03
Structure title titleCryoEM structure of gp55-dependent RNA polymerase-promoter open complex
Keywords keywordsTranscription, RNA polymerase; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.35
Radius of gyration Rg (electron density) rg_electron48.88
Forward intensity I(0) i02147890000.00
Molecular weight molecular_weight374610.0 kDa
Excluded volume excluded_volume464710 ų
Envelope volume envelope_volume688240 ų
Hydration-shell volume shell_volume112630 ų
Envelope diameter envelope_diameter166.4
Shell Rg shell_rg56.36
Envelope Rg envelope_rg48.28
Shape Rg shape_rg48.88
Total Rg total_rg49.13
Total atoms total_atoms26249
Residues n_residues3273
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 dmax157.2
Rg (real space) rg_real49.80
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.1030e+09
I(0) uncertainty (real space) i0_real_error3.3640e+07
Rg (reciprocal space) rg_reciprocal49.35
I(0) (reciprocal space) i0_reciprocal2149000000.0000
Solution quality estimate total_estimate0.7086
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.0
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.186
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha1.6450
Highest regularization parameter α highest_alpha351600000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 0.926; Sysdev: 0.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.798

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7d7cA01
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_id7d7cB01
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_id7d7cD01
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)