7pyj

CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA (NusA elongation complex in less-swiveled conformation)

Method: ELECTRON MICROSCOPY Dmax: 202.3 Å Quality: GOOD

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

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain A; UniProt 1–329 Chain B; UniProt 1–329 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ntDNA × 1 RNA × 1 tDNA × 1 Transcription termination/antitermination protein NusA × 1 (P0AFF6) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 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

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain C; UniProt 1–1342 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ntDNA × 1 RNA × 1 tDNA × 1 Transcription termination/antitermination protein NusA × 1 (P0AFF6) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain D; UniProt 1–1407 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ntDNA × 1 RNA × 1 tDNA × 1 Transcription termination/antitermination protein NusA × 1 (P0AFF6) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1407; UniProt 1–1407

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) ntDNA × 1 RNA × 1 tDNA × 1 Transcription termination/antitermination protein NusA × 1 (P0AFF6) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 E; PDBConstruct 1–91; UniProt 1–91

Transcription termination/antitermination protein NusA

Escherichia coli

UniProt P0AFF6

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 × 6 DNA 2 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain F; UniProt 1–495 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (P0A800) ntDNA × 1 RNA × 1 tDNA × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUSA_ECOLI
Isoform
PDB entities 8
Chains and sequence ranges Author chain F; PDBConstruct 1–495; UniProt 1–495

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 7pyj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7pyj
Deposition date deposition_date2021-10-10
Structure title titleCryoEM structure of E.coli RNA polymerase elongation complex bound to NusA (NusA elongation complex in less-swiveled conformation)
Keywords keywordsNusA, transcription elongation, cryo-EM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.09
Radius of gyration Rg (electron density) rg_electron53.54
Forward intensity I(0) i02828870000.00
Molecular weight molecular_weight418700.0 kDa
Excluded volume excluded_volume513620 ų
Envelope volume envelope_volume840320 ų
Hydration-shell volume shell_volume125820 ų
Envelope diameter envelope_diameter218.6
Shell Rg shell_rg59.41
Envelope Rg envelope_rg55.16
Shape Rg shape_rg53.69
Total Rg total_rg53.22
Total atoms total_atoms29362
Residues n_residues3855
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 dmax202.3
Rg (real space) rg_real54.13
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real2.8290e+09
I(0) uncertainty (real space) i0_real_error4.7510e+07
Rg (reciprocal space) rg_reciprocal54.05
I(0) (reciprocal space) i0_reciprocal2828000000.0000
Solution quality estimate total_estimate0.8198
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.8
Skewness Skewness skewness0.504
Kurtosis Kurtosis kurtosis0.178
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha561200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.565; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)