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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
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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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 3 DNA 3 ;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 ZINC ION × 2 Consistent with all polymers

Other States of the Same Protein in the Database

Monomer

None

Homodimer
1txy 1v1q 1woc 1woc 2pnh

5 assemblies

Homotetramer
1woc

1 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex
2ccz 8fak 9zbt 9zbu

4 assemblies

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 3 DNA 3 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 ZINC ION × 2 Consistent with all polymers

Other States of the Same Protein in the Database

Monomer
6dcr 6dcr

2 assemblies

Homodimer
2d7e 2d7e

2 assemblies

Homotetramer
2d7e 2d7e

2 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex
2d7g 2d7g 2d7h 2dwl 2dwl 2dwm 2dwm 2dwn 2dwn 2dwn 2dwn 8fak

14 assemblies; showing the first 12

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.

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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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8fak__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8fak__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8fak__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）35.44 Å
Rg (electron density)35.38 Å
Total Rg35.74 Å
Atom count14963
Residues894
Excluded volume133510 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8fak__assembly_1__model_1 hexameric （6） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

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7. Citations (1)