8fak

DNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli

Method: ELECTRON MICROSCOPY Dmax: 119.2 Å Quality: GOOD

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

Primosomal replication protein N

Escherichia coli (strain K12)

UniProt P07013

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 × 3 DNA 3 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–104 Chain B; UniProt 1–104 Not recorded ;DNA (5'-D(P*CP*AP*GP*AP*CP*TP*CP*AP*TP*TP*TP*AP*GP*CP*CP*CP*TP*TP*AP*TP*CP*CP*G)-3') ; × 1 ;Primosomal protein N' ; × 1 (P17888) ;DNA (5'-D(P*CP*GP*GP*AP*TP*AP*AP*GP*GP*GP*CP*TP*GP*AP*GP*CP*AP*CP*GP*CP*CP*GP*A)-3') ; × 1 ;DNA (5'-D(P*TP*CP*GP*GP*CP*GP*TP*GP*CP*TP*C)-3') ; × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRIB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–104; UniProt 1–104 Author chain B; PDBConstruct 1–104; UniProt 1–104

;Primosomal protein N' ;

Escherichia coli (strain K12)

UniProt P17888

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 × 3 DNA 3 PDB declaration: hexameric(6) Consistent with all polymer counts Chain H; UniProt 1–732 Not recorded Primosomal replication protein N × 2 (P07013) ;DNA (5'-D(P*CP*AP*GP*AP*CP*TP*CP*AP*TP*TP*TP*AP*GP*CP*CP*CP*TP*TP*AP*TP*CP*CP*G)-3') ; × 1 ;DNA (5'-D(P*CP*GP*GP*AP*TP*AP*AP*GP*GP*GP*CP*TP*GP*AP*GP*CP*AP*CP*GP*CP*CP*GP*A)-3') ; × 1 ;DNA (5'-D(P*TP*CP*GP*GP*CP*GP*TP*GP*CP*TP*C)-3') ; × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

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

View Construct and Data Evidence
UniProt name PRIA_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–732; UniProt 1–732

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 8fak

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fak
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fak
Deposition date deposition_date2022-11-28
Structure title titleDNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli
Keywords keywordsPriA, PriB, replication restart, E. coli, HELICASE-DNA complex; HELICASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.44
Radius of gyration Rg (electron density) rg_electron35.38
Forward intensity I(0) i0234525000.00
Molecular weight molecular_weight110690.0 kDa
Excluded volume excluded_volume133510 ų
Envelope volume envelope_volume190190 ų
Hydration-shell volume shell_volume46280 ų
Envelope diameter envelope_diameter128.0
Shell Rg shell_rg40.31
Envelope Rg envelope_rg35.30
Shape Rg shape_rg35.37
Total Rg total_rg35.74
Total atoms total_atoms14963
Residues n_residues894
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 dmax119.2
Rg (real space) rg_real35.52
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real2.3450e+08
I(0) uncertainty (real space) i0_real_error4.0370e+06
Rg (reciprocal space) rg_reciprocal35.48
I(0) (reciprocal space) i0_reciprocal234500000.0000
Solution quality estimate total_estimate0.8742
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30590000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.848

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)