› 5m1p

X-ray diffraction
1.1Å resolution

Crystal structure of the large terminase nuclease from thermophilic phage G20c with bound Calcium

Released:
DOI: 10.2210/pdb5m1p/pdb
PDB entry 5m1p coloured by chain, front view.
PDB entry 5m1p coloured by chain, side view.
PDB entry 5m1p coloured by chain, top view.
Source organism: Thermus phage G20c
Primary publication:
Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.
Xu RG, Jenkins HT, Chechik M, Blagova EV, Lopatina A, Klimuk E, Minakhin L, Severinov K, Greive SJ, Antson AA
OpenAccess logo Nucleic Acids Res 45 3580-3590 (2017)
PMID: 28100693

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-495828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Terminase, large subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 21.17 KDa
Source organism: Thermus phage G20c
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1L4BKS3 (Residues: 257-443; Coverage: 39%)
Gene name: G20c_80
Sequence domains: Terminase RNaseH-like domain
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 43.453Å b: 53.597Å c: 69.852Å
α: 90° β: 91.8° γ: 90°
R-values:
R R work R free
0.223 0.222 0.235
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Terminase Large Subunit Provides a New Drug Target for Herpesvirus Treatment.
Yang et al. (2019)
1 more

1 mention without citation

Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.
Xu et al. (2017)