8jo2

Structural basis of transcriptional activation by the OmpR/PhoB-family response regulator PmrA

Method: ELECTRON MICROSCOPY Dmax: 183.1 Å Quality: GOOD

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

DNA-directed RNA polymerase subunit alpha

Escherichia coli BL21(DE3)

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–329 Chain B; UniProt 1–329 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit beta × 1 (A0A140SS80) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A140NH27) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA-binding transcriptional regulator BasR × 2 (A0A0R4I965) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 3
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 BL21(DE3)

UniProt A0A140SS80

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–1342 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A140NH27) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA-binding transcriptional regulator BasR × 2 (A0A0R4I965) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 A0A140SS80_ECOBD
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–1342; UniProt 1–1342

;DNA-directed RNA polymerase subunit beta' ;

Escherichia coli BL21(DE3)

UniProt A0A140NH27

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 1–1407 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (A0A140SS80) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA-binding transcriptional regulator BasR × 2 (A0A0R4I965) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 A0A140NH27_ECOBD
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–1407; UniProt 1–1407

DNA-directed RNA polymerase subunit omega

Escherichia coli BL21(DE3)

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain E; UniProt 1–91 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (A0A140SS80) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A140NH27) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) DNA-binding transcriptional regulator BasR × 2 (A0A0R4I965) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 6
Chains and sequence ranges Author chain E; PDBConstruct 1–91; UniProt 1–91

RNA polymerase sigma factor RpoD

Escherichia coli BL21(DE3)

UniProt Q0P6L9

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 1–613 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (A0A140SS80) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A140NH27) DNA-directed RNA polymerase subunit omega × 1 (P0A800) DNA-binding transcriptional regulator BasR × 2 (A0A0R4I965) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q0P6L9_ECOLX
Isoform
PDB entities 7
Chains and sequence ranges Author chain F; PDBConstruct 1–613; UniProt 1–613

DNA-binding transcriptional regulator BasR

Klebsiella pneumoniae JM45

UniProt A0A0R4I965

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain H; UniProt 1–226 Chain I; UniProt 1–226 Not recorded DNA (65-MER) × 1 DNA (65-MER) × 1 DNA-directed RNA polymerase subunit alpha × 2 (P0A7Z4) DNA-directed RNA polymerase subunit beta × 1 (A0A140SS80) ;DNA-directed RNA polymerase subunit beta' ; × 1 (A0A140NH27) DNA-directed RNA polymerase subunit omega × 1 (P0A800) RNA polymerase sigma factor RpoD × 1 (Q0P6L9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.74 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 A0A0R4I965_KLEPN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–226; UniProt 1–226 Author chain I; PDBConstruct 1–226; UniProt 1–226

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 8jo2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8jo2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8jo2
Deposition date deposition_date2023-06-06
Structure title titleStructural basis of transcriptional activation by the OmpR/PhoB-family response regulator PmrA
Keywords keywordsPmrA, RNA polymerase, cryo-EM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.43
Radius of gyration Rg (electron density) rg_electron54.79
Forward intensity I(0) i04096050000.00
Molecular weight molecular_weight506000.0 kDa
Excluded volume excluded_volume621170 ų
Envelope volume envelope_volume919070 ų
Hydration-shell volume shell_volume134480 ų
Envelope diameter envelope_diameter194.1
Shell Rg shell_rg61.07
Envelope Rg envelope_rg54.57
Shape Rg shape_rg54.77
Total Rg total_rg54.97
Total atoms total_atoms35368
Residues n_residues4293
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 dmax183.1
Rg (real space) rg_real55.27
Rg uncertainty (real space) rg_real_error2.00
I(0) (real space) i0_real4.0960e+09
I(0) uncertainty (real space) i0_real_error9.3090e+07
Rg (reciprocal space) rg_reciprocal55.55
I(0) (reciprocal space) i0_reciprocal4098000000.0000
Solution quality estimate total_estimate0.8705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.4
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha511000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8jo2A01
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_id8jo2B01
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_id8jo2C01
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_id8jo2D01
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)