6gov

Structure of THE RNA POLYMERASE LAMBDA-BASED ANTITERMINATION COMPLEX

Method: ELECTRON MICROSCOPY Dmax: 202.7 Å Quality: GOOD

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

Transcription termination/antitermination protein NusA

Escherichia coli O157:H7

UniProt P0AFF8

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain A; UniProt 1–495 Not recorded Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUSA_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–497; UniProt 1–495

Transcription antitermination protein NusB

Escherichia coli O157:H7

UniProt P0A782

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain B; UniProt 1–139 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name NUSB_ECO57
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–141; UniProt 1–139

30S ribosomal protein S10

Escherichia coli O157:H7

UniProt P0A7R7

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain E; UniProt 1–103 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RS10_ECO57
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 4–106; UniProt 1–103

Transcription termination/antitermination protein NusG

Escherichia coli O157:H7

UniProt P0AFG1

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain G; UniProt 1–181 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUSG_ECO57
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 4–184; UniProt 1–181

Antitermination protein N

Escherichia phage lambda

UniProt P03045

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain N; UniProt 1–107 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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

View Construct and Data Evidence
UniProt name REGN_LAMBD
Isoform
PDB entities 5
Chains and sequence ranges Author chain N; PDBConstruct 4–110; UniProt 1–107

DNA-directed RNA polymerase subunit alpha

Escherichia coli O157:H7

UniProt P0A7Z6

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain U; UniProt 1–329 Chain V; UniProt 1–329 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

32 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECO57
Isoform
PDB entities 6
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 O157:H7

UniProt P0A802

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain W; UniProt 1–91 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECO57
Isoform
PDB entities 7
Chains and sequence ranges Author chain W; PDBConstruct 1–91; UniProt 1–91

DNA-directed RNA polymerase subunit beta

Escherichia coli O157:H7

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain X; UniProt 1–1342 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 8
Chains and sequence ranges Author chain X; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli O157:H7

UniProt P0A8T8

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 × 10 DNA 2 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain Y; UniProt 1–1407 Not recorded Transcription termination/antitermination protein NusA × 1 (P0AFF8) Transcription antitermination protein NusB × 1 (P0A782) 30S ribosomal protein S10 × 1 (P0A7R7) Transcription termination/antitermination protein NusG × 1 (P0AFG1) Antitermination protein N × 1 (P03045) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit omega × 1 (P0A802) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) DNA (I) × 1 DNA (II) × 1 RNA (TRANSCRIPTION BUBBLE) × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

51 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_ECO57
Isoform
PDB entities 9
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 6gov

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6gov
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6gov
Deposition date deposition_date2018-06-04
Structure title titleStructure of THE RNA POLYMERASE LAMBDA-BASED ANTITERMINATION COMPLEX
Keywords keywords;TRANSCRIPTION/DNA/RNA, DNA-DEPENDENT RNA POLYMERASE, BACTERIAL TRANSCRIPTION, TERNARY ELONGATION COMPLEX, ANTITERMINATION, TRANSCRIPTION-DNA-RNA COMPLEX, transcription ;; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.80
Radius of gyration Rg (electron density) rg_electron60.20
Forward intensity I(0) i03988130000.00
Molecular weight molecular_weight500970.0 kDa
Excluded volume excluded_volume615740 ų
Envelope volume envelope_volume989890 ų
Hydration-shell volume shell_volume137450 ų
Envelope diameter envelope_diameter220.5
Shell Rg shell_rg62.09
Envelope Rg envelope_rg59.52
Shape Rg shape_rg60.23
Total Rg total_rg60.15
Total atoms total_atoms35040
Residues n_residues4274
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 dmax202.7
Rg (real space) rg_real59.90
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real3.9880e+09
I(0) uncertainty (real space) i0_real_error8.5940e+07
Rg (reciprocal space) rg_reciprocal59.70
I(0) (reciprocal space) i0_reciprocal3987000000.0000
Solution quality estimate total_estimate0.7996
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.2
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.191
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha550900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id6govA01
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_id6govA02
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_id6govA03
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_id6govE00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily600 — Ribosomal protein S10
Domain ID domain_id6govU01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id6govU02
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_id6govV01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id6govV02
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_id6govW00
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
Domain ID domain_id6govY01
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)