7d7d

CryoEM structure of gp45-dependent transcription activation complex

Method: ELECTRON MICROSCOPY Dmax: 198.1 Å Quality: GOOD

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 × 10 DNA 2 PDB declaration: dodecameric(12) 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 RNA polymerase-associated protein Gp33 × 1 (P13338) DNA-directed RNA polymerase subunit omega × 1 (A0A070UPX4) DNA polymerase clamp × 3 (P04525) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 × 10 DNA 2 PDB declaration: dodecameric(12) 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 RNA polymerase-associated protein Gp33 × 1 (P13338) DNA-directed RNA polymerase subunit omega × 1 (A0A070UPX4) DNA polymerase clamp × 3 (P04525) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 × 10 DNA 2 PDB declaration: dodecameric(12) 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 RNA polymerase-associated protein Gp33 × 1 (P13338) DNA-directed RNA polymerase subunit omega × 1 (A0A070UPX4) DNA polymerase clamp × 3 (P04525) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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

RNA polymerase-associated protein Gp33

Enterobacteria phage T4

UniProt P13338

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 1–112 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (U9ZUN7) 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 DNA-directed RNA polymerase subunit omega × 1 (A0A070UPX4) DNA polymerase clamp × 3 (P04525) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 VG33_BPT4
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 21–132; UniProt 1–112

DNA-directed RNA polymerase subunit omega

Escherichia coli

UniProt A0A070UPX4

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (U9ZUN7) 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 RNA polymerase-associated protein Gp33 × 1 (P13338) DNA polymerase clamp × 3 (P04525) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 A0A070UPX4_ECOLX
Isoform
PDB entities 8
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 1–91

DNA polymerase clamp

Enterobacteria phage T4

UniProt P04525

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain G; UniProt 1–228 Chain H; UniProt 1–228 Chain I; UniProt 1–228 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (U9ZUN7) 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 RNA polymerase-associated protein Gp33 × 1 (P13338) DNA-directed RNA polymerase subunit omega × 1 (A0A070UPX4) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPA5_BPT4
Isoform
PDB entities 9
Chains and sequence ranges Author chain G; PDBConstruct 1–228; UniProt 1–228 Author chain H; PDBConstruct 1–228; UniProt 1–228 Author chain I; PDBConstruct 1–228; UniProt 1–228

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 7d7d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d7d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d7d
Deposition date deposition_date2020-10-03
Structure title titleCryoEM structure of gp45-dependent transcription activation 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_guinier57.47
Radius of gyration Rg (electron density) rg_electron57.37
Forward intensity I(0) i03571790000.00
Molecular weight molecular_weight482100.0 kDa
Excluded volume excluded_volume595930 ų
Envelope volume envelope_volume921780 ų
Hydration-shell volume shell_volume132150 ų
Envelope diameter envelope_diameter196.8
Shell Rg shell_rg61.07
Envelope Rg envelope_rg56.50
Shape Rg shape_rg57.39
Total Rg total_rg57.39
Total atoms total_atoms33755
Residues n_residues4170
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 dmax198.1
Rg (real space) rg_real57.37
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real3.5720e+09
I(0) uncertainty (real space) i0_real_error6.7310e+07
Rg (reciprocal space) rg_reciprocal57.53
I(0) (reciprocal space) i0_reciprocal3573000000.0000
Solution quality estimate total_estimate0.8633
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha463400000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)