› 2ge5

X-ray diffraction
2.4Å resolution

EcoRV Restriction Endonuclease C-terminal deletion mutant/GATATC/Ca2+

Released:
DOI: 10.2210/pdb2ge5/pdb
PDB entry 2ge5 coloured by chain, front view.
PDB entry 2ge5 coloured by chain, side view.
PDB entry 2ge5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Positively charged C-terminal subdomains of EcoRV endonuclease: contributions to DNA binding, bending, and cleavage.
Hiller DA, Perona JJ
Biochemistry 45 11453-63 (2006)
PMID: 16981705

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-115294 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Type II restriction enzyme EcoRV Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 25.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04390 (Residues: 2-220; Coverage: 89%)
Gene name: ecoRVR
Sequence domains: Restriction endonuclease EcoRV
Structure domains: DNA mismatch repair MutH/Restriction endonuclease, type II
5'-D(*AP*AP*AP*GP*AP*TP*AP*TP*CP*TP*T)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 nucleotides
Theoretical weight: 3.36 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P43212
Unit cell:
a: 67.101Å b: 67.101Å c: 259.892Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.284
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Type II restriction endonucleases--a historical perspective and more.
Pingoud et al. (2014)
4 other articles

1 mention without citation

Positively charged C-terminal subdomains of EcoRV endonuclease: contributions to DNA binding, bending, and cleavage.
Hiller et al. (2006)