9q92

CryoEM structure of bacterial transcription intermediate complex mediated by activator PspF containing nifH promoter DNA containing mismatch from -11 to -8 - conformation 5

Method: ELECTRON MICROSCOPY Dmax: 238.7 Å Quality: GOOD

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

Psp operon transcriptional activator

Escherichia coli K-12

UniProt P37344

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 1; UniProt 1–259 Chain 2; UniProt 1–259 Chain 3; UniProt 1–259 Chain 4; UniProt 1–259 Chain 5; UniProt 1–259 Chain 6; UniProt 1–259 Not recorded Template DNA (34-MER) × 1 RNA polymerase sigma-54 factor × 1 (A0A377VEN9) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSPF_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–259; UniProt 1–259 Author chain 2; PDBConstruct 1–259; UniProt 1–259 Author chain 3; PDBConstruct 1–259; UniProt 1–259 Author chain 4; PDBConstruct 1–259; UniProt 1–259 Author chain 5; PDBConstruct 1–259; UniProt 1–259 Author chain 6; PDBConstruct 1–259; UniProt 1–259

RNA polymerase sigma-54 factor

Klebsiella pneumoniae

UniProt A0A377VEN9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain M; UniProt 2–453 Not recorded Template DNA (34-MER) × 1 Psp operon transcriptional activator × 6 (P37344) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A377VEN9_KLEPN
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 24–475; UniProt 2–453

DNA-directed RNA polymerase subunit alpha

Escherichia coli K-12

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 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–329 Chain B; UniProt 1–329 Not recorded Template DNA (34-MER) × 1 Psp operon transcriptional activator × 6 (P37344) RNA polymerase sigma-54 factor × 1 (A0A377VEN9) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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 A; PDBConstruct 1–329; UniProt 1–329 Author chain B; PDBConstruct 1–329; UniProt 1–329

DNA-directed RNA polymerase subunit beta

Escherichia coli K-12

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 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 1–1341 Not recorded Template DNA (34-MER) × 1 Psp operon transcriptional activator × 6 (P37344) RNA polymerase sigma-54 factor × 1 (A0A377VEN9) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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 C; PDBConstruct 1–1341; UniProt 1–1341

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli K-12

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 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 1–1407 Not recorded Template DNA (34-MER) × 1 Psp operon transcriptional activator × 6 (P37344) RNA polymerase sigma-54 factor × 1 (A0A377VEN9) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) DNA-directed RNA polymerase subunit omega × 1 (P0A800) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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 D; PDBConstruct 1–1407; UniProt 1–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli K-12

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 Protein–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded Template DNA (34-MER) × 1 Psp operon transcriptional activator × 6 (P37344) RNA polymerase sigma-54 factor × 1 (A0A377VEN9) DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (P0A8V2) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P0A8T7) Non-template DNA (34-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 AF3 ALUMINUM FLUORIDE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.80 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 E; PDBConstruct 1–91; UniProt 1–91

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 9q92

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q92
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q92
Deposition date deposition_date2025-02-26
最后修订 last_revision2025-07-16
Structure title titleCryoEM structure of bacterial transcription intermediate complex mediated by activator PspF containing nifH promoter DNA containing mismatch from -11 to -8 - conformation 5
Keywords keywordssigma factor, transcription, complex, AAA+, DNA-binding protein; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.91
Radius of gyration Rg (electron density) rg_electron68.26
Forward intensity I(0) i03181090000.00
Molecular weight molecular_weight376670.0 kDa
Excluded volume excluded_volume428070 ų
Envelope volume envelope_volume1012600 ų
Hydration-shell volume shell_volume128490 ų
Envelope diameter envelope_diameter239.9
Shell Rg shell_rg65.90
Envelope Rg envelope_rg65.02
Shape Rg shape_rg68.27
Total Rg total_rg68.17
Total atoms total_atoms26767
Residues n_residues5183
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 dmax238.7
Rg (real space) rg_real68.00
Rg uncertainty (real space) rg_real_error2.27
I(0) (real space) i0_real3.1810e+09
I(0) uncertainty (real space) i0_real_error6.5440e+07
Rg (reciprocal space) rg_reciprocal67.53
I(0) (reciprocal space) i0_reciprocal3178000000.0000
Solution quality estimate total_estimate0.8481
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.6
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha334600000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)