8gj1

E. coli clamp loader with open clamp on primed template DNA (form 2)

Method: ELECTRON MICROSCOPY Dmax: 136.9 Å Quality: GOOD

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

DNA polymerase III subunit delta

Escherichia coli K-12

UniProt P28630

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 1–343 Not recorded DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) DNA polymerase III subunit psi × 1 (P28632) Beta sliding clamp × 2 (P0A988) Primer × 1 Template × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ALF TETRAFLUOROALUMINATE ION × 3 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;30 mM Tris-HCl pH 7.6, 5 mM MgCl2, 2 mM ADP, 0.5 mM AlCl3, 5 mM NaF, 5 mM dithiothreitol, 0.25 mM EDTA, 2% glycerol. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied onto a Ultrafoil Au R1.2/1.3 grid. Blot for 4.5 s with no extra force before plunging into liquid ethane. Resolution 3.00 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.

35 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–343; UniProt 1–343

DNA polymerase III subunit tau

Escherichia coli K-12

UniProt P06710

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 B; UniProt 1–643 Chain C; UniProt 1–643 Chain D; UniProt 1–643 Not recorded DNA polymerase III subunit delta × 1 (P28630) ;DNA polymerase III subunit delta' ; × 1 (P28631) DNA polymerase III subunit psi × 1 (P28632) Beta sliding clamp × 2 (P0A988) Primer × 1 Template × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ALF TETRAFLUOROALUMINATE ION × 3 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;30 mM Tris-HCl pH 7.6, 5 mM MgCl2, 2 mM ADP, 0.5 mM AlCl3, 5 mM NaF, 5 mM dithiothreitol, 0.25 mM EDTA, 2% glycerol. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied onto a Ultrafoil Au R1.2/1.3 grid. Blot for 4.5 s with no extra force before plunging into liquid ethane. Resolution 3.00 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.

38 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3X_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–643; UniProt 1–643 Author chain C; PDBConstruct 1–643; UniProt 1–643 Author chain D; PDBConstruct 1–643; UniProt 1–643

;DNA polymerase III subunit delta' ;

Escherichia coli K-12

UniProt P28631

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 1–334 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) DNA polymerase III subunit psi × 1 (P28632) Beta sliding clamp × 2 (P0A988) Primer × 1 Template × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ALF TETRAFLUOROALUMINATE ION × 3 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;30 mM Tris-HCl pH 7.6, 5 mM MgCl2, 2 mM ADP, 0.5 mM AlCl3, 5 mM NaF, 5 mM dithiothreitol, 0.25 mM EDTA, 2% glycerol. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied onto a Ultrafoil Au R1.2/1.3 grid. Blot for 4.5 s with no extra force before plunging into liquid ethane. Resolution 3.00 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.

34 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLB_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–334; UniProt 1–334

DNA polymerase III subunit psi

Escherichia coli K-12

UniProt P28632

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 1–137 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) Beta sliding clamp × 2 (P0A988) Primer × 1 Template × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ALF TETRAFLUOROALUMINATE ION × 3 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;30 mM Tris-HCl pH 7.6, 5 mM MgCl2, 2 mM ADP, 0.5 mM AlCl3, 5 mM NaF, 5 mM dithiothreitol, 0.25 mM EDTA, 2% glycerol. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied onto a Ultrafoil Au R1.2/1.3 grid. Blot for 4.5 s with no extra force before plunging into liquid ethane. Resolution 3.00 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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–137; UniProt 1–137

Beta sliding clamp

Escherichia coli K-12

UniProt P0A988

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 1–366 Chain I; UniProt 1–366 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) DNA polymerase III subunit psi × 1 (P28632) Primer × 1 Template × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ALF TETRAFLUOROALUMINATE ION × 3 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;30 mM Tris-HCl pH 7.6, 5 mM MgCl2, 2 mM ADP, 0.5 mM AlCl3, 5 mM NaF, 5 mM dithiothreitol, 0.25 mM EDTA, 2% glycerol. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample was applied onto a Ultrafoil Au R1.2/1.3 grid. Blot for 4.5 s with no extra force before plunging into liquid ethane. Resolution 3.00 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.

53 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3B_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–366; UniProt 1–366 Author chain I; PDBConstruct 1–366; UniProt 1–366

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 8gj1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8gj1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8gj1
Deposition date deposition_date2023-03-14
Structure title titleE. coli clamp loader with open clamp on primed template DNA (form 2)
Keywords keywordsclamp loader, DNA clamp, AAA+, ATPase, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.15
Radius of gyration Rg (electron density) rg_electron43.66
Forward intensity I(0) i01430470000.00
Molecular weight molecular_weight300120.0 kDa
Excluded volume excluded_volume370610 ų
Envelope volume envelope_volume535750 ų
Hydration-shell volume shell_volume96947 ų
Envelope diameter envelope_diameter144.2
Shell Rg shell_rg53.01
Envelope Rg envelope_rg42.39
Shape Rg shape_rg43.67
Total Rg total_rg43.99
Total atoms total_atoms41571
Residues n_residues2591
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 dmax136.9
Rg (real space) rg_real43.87
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.4300e+09
I(0) uncertainty (real space) i0_real_error2.6450e+07
Rg (reciprocal space) rg_reciprocal44.15
I(0) (reciprocal space) i0_reciprocal1431000000.0000
Solution quality estimate total_estimate0.8862
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.0
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha267900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)