› 1v33

X-ray diffraction
1.8Å resolution

Crystal structure of DNA primase from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb1v33/pdb
PDB entry 1v33 coloured by chain, front view.
PDB entry 1v33 coloured by chain, side view.
PDB entry 1v33 coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis.
Ito N, Nureki O, Shirouzu M, Yokoyama S, Hanaoka F
Genes Cells 8 913-23 (2003)
PMID: 14750947

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129634 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA primase small subunit PriS Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 42.64 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O57934 (Residues: 1-346; Coverage: 100%)
Gene names: PH0195, priA, priS
Sequence domains: DNA primase small subunit
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 76.451Å b: 76.451Å c: 128.894Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.219 0.244
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Bacterial DNA repair by non-homologous end joining.
Shuman et al. (2007)
6 more

5 mentions without citation

Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.
Guilliam et al. (2015)
4 more