6alf

CryoEM structure of crosslinked E.coli RNA polymerase elongation complex

Method: ELECTRON MICROSCOPY Dmax: 151.4 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli (strain K12)

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain G; UniProt 1–234 Chain H; UniProt 1–234 Not recorded ;DNA (5'-D(*GP*GP*GP*CP*TP*AP*AP*TP*GP*AP*CP*GP*GP*CP*GP*AP*AP*TP*AP*CP*CP*C)-3') ; × 1 DNA (29-MER) × 1 ;RNA (5'-R(P*AP*GP*CP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH8.0, 150 mM KCl, 5mM MgCl2, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 4
Chains and sequence ranges Author chain G; PDBConstruct 1–234; UniProt 1–234 Author chain H; PDBConstruct 1–234; UniProt 1–234

DNA-directed RNA polymerase subunit beta

Escherichia coli (strain K12)

UniProt P0A8V2

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain I; UniProt 1–1342 Not recorded ;DNA (5'-D(*GP*GP*GP*CP*TP*AP*AP*TP*GP*AP*CP*GP*GP*CP*GP*AP*AP*TP*AP*CP*CP*C)-3') ; × 1 DNA (29-MER) × 1 ;RNA (5'-R(P*AP*GP*CP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH8.0, 150 mM KCl, 5mM MgCl2, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

219 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

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

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli (strain K12)

UniProt P0A8T7

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain J; UniProt 1–1407 Not recorded ;DNA (5'-D(*GP*GP*GP*CP*TP*AP*AP*TP*GP*AP*CP*GP*GP*CP*GP*AP*AP*TP*AP*CP*CP*C)-3') ; × 1 DNA (29-MER) × 1 ;RNA (5'-R(P*AP*GP*CP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH8.0, 150 mM KCl, 5mM MgCl2, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

239 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–1407; UniProt 1–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli (strain K12)

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 × 5 DNA 2 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain K; UniProt 1–80 Not recorded ;DNA (5'-D(*GP*GP*GP*CP*TP*AP*AP*TP*GP*AP*CP*GP*GP*CP*GP*AP*AP*TP*AP*CP*CP*C)-3') ; × 1 DNA (29-MER) × 1 ;RNA (5'-R(P*AP*GP*CP*GP*GP*AP*GP*AP*GP*GP*UP*A)-3') ; × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH8.0, 150 mM KCl, 5mM MgCl2, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 7
Chains and sequence ranges Author chain K; PDBConstruct 1–80; UniProt 1–80

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 6alf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6alf
Deposition date deposition_date2017-08-07
Structure title titleCryoEM structure of crosslinked E.coli RNA polymerase elongation complex
Keywords keywordsDNA-dependent RNA polymerase, TRANSCRIPTION, transcription-dna-rna complex; transcription/dna/rna
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.35
Radius of gyration Rg (electron density) rg_electron47.13
Forward intensity I(0) i02179170000.00
Molecular weight molecular_weight373140.0 kDa
Excluded volume excluded_volume461150 ų
Envelope volume envelope_volume666270 ų
Hydration-shell volume shell_volume110910 ų
Envelope diameter envelope_diameter163.8
Shell Rg shell_rg55.97
Envelope Rg envelope_rg47.07
Shape Rg shape_rg47.14
Total Rg total_rg47.38
Total atoms total_atoms26123
Residues n_residues3237
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 dmax151.4
Rg (real space) rg_real47.12
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real2.1790e+09
I(0) uncertainty (real space) i0_real_error3.6570e+07
Rg (reciprocal space) rg_reciprocal47.35
I(0) (reciprocal space) i0_reciprocal2180000000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.6
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.333
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha489600000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.826

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)