› 8q3r

Electron Microscopy
3.8Å resolution

Cryo-EM structure of the DNA polymerase holoenzyme E9-A20-D4 of vaccinia virus

Released:
DOI: 10.2210/pdb8q3r/pdb
PDB entry 8q3r coloured by chain, front view.
PDB entry 8q3r coloured by chain, side view.
PDB entry 8q3r coloured by chain, top view.
Source organism: Vaccinia virus Copenhagen
Primary publication:
Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus.
Burmeister WP, Boutin L, Balestra AC, Gröger H, Ballandras-Colas A, Hutin S, Kraft C, Grimm C, Böttcher B, Fischer U, Tarbouriech N, Iseni F
PLoS Pathog 20 e1011652 (2024)
PMID: 38768256
Related structures: EMD-18134

Function and Biology Details

Reactions catalysed: 
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-273339 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Uracil-DNA glycosylase Chain: D
Molecule details ›
Chain: D
Length: 242 amino acids
Theoretical weight: 27.47 KDa
Source organism: Vaccinia virus Copenhagen
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P20536 (Residues: 1-218; Coverage: 100%)
Gene names: D4R, OPG116, UNG
DNA polymerase processivity factor component OPG148 Chain: A
Molecule details ›
Chain: A
Length: 426 amino acids
Theoretical weight: 49.25 KDa
Source organism: Vaccinia virus Copenhagen
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P20995 (Residues: 1-426; Coverage: 100%)
Gene names: A20R, OPG148
Sequence domains: Chordopoxvirus A20R protein
DNA polymerase Chain: E

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-18134
Expression system: Trichoplusia ni

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