6xll

Cryo-EM structure of E. coli RNAP-promoter initial transcribing complex with 5-nt RNA transcript (RPitc-5nt)

Method: ELECTRON MICROSCOPY Dmax: 171.2 Å Quality: GOOD

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

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 × 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 (B7MIX3) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (B7MFL0) RNA polymerase sigma factor RpoD × 1 (P00579) synthetic non-template strand DNA (54-MER) × 1 synthetic template strand DNA (54-MER) × 1 RNA transcript (5-MER) × 1 1N7 CHAPSO × 2 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 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 O157:H7

UniProt B7MIX3

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 (P0A7Z6) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (B7MFL0) RNA polymerase sigma factor RpoD × 1 (P00579) synthetic non-template strand DNA (54-MER) × 1 synthetic template strand DNA (54-MER) × 1 RNA transcript (5-MER) × 1 1N7 CHAPSO × 2 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

18 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_ECO45
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 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 × 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 (P0A7Z6) DNA-directed RNA polymerase subunit beta × 1 (B7MIX3) DNA-directed RNA polymerase subunit omega × 1 (B7MFL0) RNA polymerase sigma factor RpoD × 1 (P00579) synthetic non-template strand DNA (54-MER) × 1 synthetic template strand DNA (54-MER) × 1 RNA transcript (5-MER) × 1 1N7 CHAPSO × 2 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1407; UniProt 1–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli O157:H7

UniProt B7MFL0

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 (P0A7Z6) DNA-directed RNA polymerase subunit beta × 1 (B7MIX3) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) RNA polymerase sigma factor RpoD × 1 (P00579) synthetic non-template strand DNA (54-MER) × 1 synthetic template strand DNA (54-MER) × 1 RNA transcript (5-MER) × 1 1N7 CHAPSO × 2 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_ECO45
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 1–91

RNA polymerase sigma factor RpoD

Escherichia coli O157:H7

UniProt P00579

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 1–613 Not recorded DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z6) DNA-directed RNA polymerase subunit beta × 1 (B7MIX3) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T8) DNA-directed RNA polymerase subunit omega × 1 (B7MFL0) synthetic non-template strand DNA (54-MER) × 1 synthetic template strand DNA (54-MER) × 1 RNA transcript (5-MER) × 1 1N7 CHAPSO × 2 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

91 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOD_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–613; UniProt 1–613

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 6xll

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xll
Deposition date deposition_date2020-06-28
Structure title titleCryo-EM structure of E. coli RNAP-promoter initial transcribing complex with 5-nt RNA transcript (RPitc-5nt)
Keywords keywordsTranscriptional factor, TRANSCRIPTION, TRANSFERASE-DNA complex, promoter escape, multidrug recognition; TRANSCRIPTION, TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.83
Radius of gyration Rg (electron density) rg_electron51.35
Forward intensity I(0) i03153780000.00
Molecular weight molecular_weight445350.0 kDa
Excluded volume excluded_volume547920 ų
Envelope volume envelope_volume789410 ų
Hydration-shell volume shell_volume122510 ų
Envelope diameter envelope_diameter184.3
Shell Rg shell_rg58.38
Envelope Rg envelope_rg51.49
Shape Rg shape_rg51.35
Total Rg total_rg51.54
Total atoms total_atoms31134
Residues n_residues3785
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 dmax171.2
Rg (real space) rg_real51.70
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real3.1540e+09
I(0) uncertainty (real space) i0_real_error5.8830e+07
Rg (reciprocal space) rg_reciprocal51.92
I(0) (reciprocal space) i0_reciprocal3155000000.0000
Solution quality estimate total_estimate0.8680
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.8
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.240
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha440200000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6xllA01
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_id6xllB01
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_id6xllC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily150 — RNA polymerase II, Rpb2 subunit, wall domain
Domain ID domain_id6xllD01
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)