5m1s

Cryo-EM structure of the E. coli replicative DNA polymerase-clamp-exonuclase-theta complex bound to DNA in the editing mode

Method: ELECTRON MICROSCOPY Dmax: 139.5 Å Quality: GOOD

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

DNA polymerase III subunit alpha

Escherichia coli K12

UniProt P10443

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–927 Mutation:A921L, M923L DNA polymerase III subunit beta × 2 (P0A988) DNA polymerase III subunit epsilon × 1 (P03007) DNA Primer Strand × 1 DNA Template Strand × 1 DNA polymerase III subunit theta × 1 (P0ABS8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Prior to sample preparation 0.1 volumes of 0.05% Tween 20 were added to the sample 3 microliters were pipetted onto the grid and blotted for 4 seconds Resolution 6.70 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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3A_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–927; UniProt 1–927

DNA polymerase III subunit beta

Escherichia coli K12

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain B; UniProt 1–366 Chain C; UniProt 1–366 Not recorded DNA polymerase III subunit alpha × 1 (P10443) DNA polymerase III subunit epsilon × 1 (P03007) DNA Primer Strand × 1 DNA Template Strand × 1 DNA polymerase III subunit theta × 1 (P0ABS8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Prior to sample preparation 0.1 volumes of 0.05% Tween 20 were added to the sample 3 microliters were pipetted onto the grid and blotted for 4 seconds Resolution 6.70 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–366; UniProt 1–366 Author chain C; PDBConstruct 1–366; UniProt 1–366

DNA polymerase III subunit epsilon

Escherichia coli K12

UniProt P03007

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain D; UniProt 1–243 Mutation:T183L M185L A186P F187L DNA polymerase III subunit alpha × 1 (P10443) DNA polymerase III subunit beta × 2 (P0A988) DNA Primer Strand × 1 DNA Template Strand × 1 DNA polymerase III subunit theta × 1 (P0ABS8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Prior to sample preparation 0.1 volumes of 0.05% Tween 20 were added to the sample 3 microliters were pipetted onto the grid and blotted for 4 seconds Resolution 6.70 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.

10 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3E_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–243; UniProt 1–243

DNA polymerase III subunit theta

Escherichia coli K12

UniProt P0ABS8

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain F; UniProt 10–65 Not recorded DNA polymerase III subunit alpha × 1 (P10443) DNA polymerase III subunit beta × 2 (P0A988) DNA polymerase III subunit epsilon × 1 (P03007) DNA Primer Strand × 1 DNA Template Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Prior to sample preparation 0.1 volumes of 0.05% Tween 20 were added to the sample 3 microliters were pipetted onto the grid and blotted for 4 seconds Resolution 6.70 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 HOLE_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–56; UniProt 10–65

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 5m1s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5m1s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5m1s
Deposition date deposition_date2016-10-10
Structure title titleCryo-EM structure of the E. coli replicative DNA polymerase-clamp-exonuclase-theta complex bound to DNA in the editing mode
Keywords keywordsDNA editing Proofreading Exonuclease Polymerase, DNA Binding protein; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.65
Radius of gyration Rg (electron density) rg_electron43.58
Forward intensity I(0) i0825332000.00
Molecular weight molecular_weight228710.0 kDa
Excluded volume excluded_volume282930 ų
Envelope volume envelope_volume409300 ų
Hydration-shell volume shell_volume76773 ų
Envelope diameter envelope_diameter138.9
Shell Rg shell_rg50.45
Envelope Rg envelope_rg42.05
Shape Rg shape_rg43.61
Total Rg total_rg43.81
Total atoms total_atoms16020
Residues n_residues1983
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 dmax139.5
Rg (real space) rg_real43.45
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real8.2530e+08
I(0) uncertainty (real space) i0_real_error1.5430e+07
Rg (reciprocal space) rg_reciprocal43.65
I(0) (reciprocal space) i0_reciprocal825500000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87170000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)