7adc

Transcription termination intermediate complex 3 delta NusG

Method: ELECTRON MICROSCOPY Dmax: 255.2 Å Quality: GOOD

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

Transcription termination factor Rho

Escherichia coli

UniProt A0A0A0GPI6

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain a; UniProt 25–443 Chain b; UniProt 25–443 Chain c; UniProt 25–443 Chain d; UniProt 25–443 Chain e; UniProt 25–443 Chain f; UniProt 25–443 Not recorded Transcription termination/antitermination protein NusA × 1 (C3SSN7) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (C3SIA2) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0A0GPI6_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain a; PDBConstruct 1–419; UniProt 25–443 Author chain b; PDBConstruct 1–419; UniProt 25–443 Author chain c; PDBConstruct 1–419; UniProt 25–443 Author chain d; PDBConstruct 1–419; UniProt 25–443 Author chain e; PDBConstruct 1–419; UniProt 25–443 Author chain f; PDBConstruct 1–419; UniProt 25–443

Transcription termination/antitermination protein NusA

Escherichia coli

UniProt C3SSN7

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain A; UniProt 1–495 Not recorded Transcription termination factor Rho × 6 (A0A0A0GPI6) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (C3SIA2) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SSN7_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 3–497; UniProt 1–495

DNA-directed RNA polymerase subunit alpha

Escherichia coli

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain U; UniProt 1–329 Chain V; UniProt 1–329 Not recorded Transcription termination factor Rho × 6 (A0A0A0GPI6) Transcription termination/antitermination protein NusA × 1 (C3SSN7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (C3SIA2) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 3
Chains and sequence ranges Author chain U; PDBConstruct 1–329; UniProt 1–329 Author chain V; PDBConstruct 1–329; UniProt 1–329

DNA-directed RNA polymerase subunit omega

Escherichia coli

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain W; UniProt 1–91 Not recorded Transcription termination factor Rho × 6 (A0A0A0GPI6) Transcription termination/antitermination protein NusA × 1 (C3SSN7) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (C3SIA2) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 W; PDBConstruct 1–91; UniProt 1–91

DNA-directed RNA polymerase subunit beta

Escherichia coli

UniProt P0A8V4

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain X; UniProt 1–1342 Not recorded Transcription termination factor Rho × 6 (A0A0A0GPI6) Transcription termination/antitermination protein NusA × 1 (C3SSN7) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ;DNA-directed RNA polymerase subunit beta' ; × 1 (C3SIA2) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

113 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECO57
Isoform
PDB entities 5
Chains and sequence ranges Author chain X; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

UniProt C3SIA2

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 × 12 DNA 2 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain Y; UniProt 1–1407 Not recorded Transcription termination factor Rho × 6 (A0A0A0GPI6) Transcription termination/antitermination protein NusA × 1 (C3SSN7) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ntDNA × 1 tDNA × 1 rut RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 6 BEF BERYLLIUM TRIFLUORIDE ION × 5 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SIA2_ECOLX
Isoform
PDB entities 6
Chains and sequence ranges Author chain Y; 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 7adc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7adc
Deposition date deposition_date2020-09-14
Structure title titleTranscription termination intermediate complex 3 delta NusG
Keywords keywordsRNA Polymerase, Rho, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.68
Radius of gyration Rg (electron density) rg_electron65.79
Forward intensity I(0) i08081890000.00
Molecular weight molecular_weight736160.0 kDa
Excluded volume excluded_volume912720 ų
Envelope volume envelope_volume1440300 ų
Hydration-shell volume shell_volume177560 ų
Envelope diameter envelope_diameter237.2
Shell Rg shell_rg70.68
Envelope Rg envelope_rg64.39
Shape Rg shape_rg65.80
Total Rg total_rg65.85
Total atoms total_atoms51550
Residues n_residues6417
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 dmax255.2
Rg (real space) rg_real69.93
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real8.1680e+09
I(0) uncertainty (real space) i0_real_error1.6950e+08
Rg (reciprocal space) rg_reciprocal65.75
I(0) (reciprocal space) i0_reciprocal8084000000.0000
Solution quality estimate total_estimate0.8629
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.4
Skewness Skewness skewness0.679
Kurtosis Kurtosis kurtosis0.507
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.8267
Highest regularization parameter α highest_alpha964400000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.627; Stabil: 0.839; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id7adcA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1480 — N Utilization Substance Protein A; Chain:P; domain 4
Homologous superfamily homologous superfamily10 — NusA, N-terminal domain
Domain ID domain_id7adcA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id7adcA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain
Domain ID domain_id7adcU01
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_id7adcV01
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_id7adcY01
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_id7adca01
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_id7adcb01
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_id7adcc01
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_id7adcd01
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_id7adce01
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_id7adcf01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)