8g5j

Cryo-EM structure of the Mismatch Uncoupling Complex (II) of Human Mitochondrial DNA Polymerase Gamma

Method: ELECTRON MICROSCOPY Dmax: 135.2 Å Quality: GOOD

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

DNA polymerase subunit gamma-1

Homo sapiens

UniProt P54098

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 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 1–1239 Not recorded DNA polymerase subunit gamma-2, mitochondrial × 2 (Q9UHN1) Mismatched Primer DNA × 1 Template DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;10 mM Tris-Hcl pH 7.9, 100 mM Nacl, 10 mM DTT, and 2 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.63 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 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1239; UniProt 1–1239

DNA polymerase subunit gamma-2, mitochondrial

Homo sapiens

UniProt Q9UHN1

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 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain B; UniProt 1–485 Chain C; UniProt 1–485 Not recorded DNA polymerase subunit gamma-1 × 1 (P54098) Mismatched Primer DNA × 1 Template DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;10 mM Tris-Hcl pH 7.9, 100 mM Nacl, 10 mM DTT, and 2 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.63 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.

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

View Construct and Data Evidence
UniProt name DPOG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–485; UniProt 1–485 Author chain C; PDBConstruct 1–485; UniProt 1–485

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 8g5j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g5j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g5j
Deposition date deposition_date2023-02-13
最后修订 last_revision2024-01-10
Structure title titleCryo-EM structure of the Mismatch Uncoupling Complex (II) of Human Mitochondrial DNA Polymerase Gamma
Keywords keywordsMitochondrial DNA Polymerase, DNA Proofreading, PolG, REPLICATION, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.23
Radius of gyration Rg (electron density) rg_electron40.85
Forward intensity I(0) i0685186000.00
Molecular weight molecular_weight206940.0 kDa
Excluded volume excluded_volume255580 ų
Envelope volume envelope_volume351840 ų
Hydration-shell volume shell_volume69978 ų
Envelope diameter envelope_diameter146.9
Shell Rg shell_rg47.55
Envelope Rg envelope_rg40.53
Shape Rg shape_rg40.86
Total Rg total_rg41.15
Total atoms total_atoms14524
Residues n_residues1778
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 dmax135.2
Rg (real space) rg_real41.18
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real6.8520e+08
I(0) uncertainty (real space) i0_real_error1.1130e+07
Rg (reciprocal space) rg_reciprocal41.23
I(0) (reciprocal space) i0_reciprocal685200000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.3
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96820000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)