1pov

X-ray diffraction
2.8Å resolution

ROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero 180-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136698 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein VP0 Chain: 0
Molecule details ›
Chain: 0
Length: 340 amino acids
Theoretical weight: 37.45 KDa
Source organism: Human poliovirus 1 Mahoney
UniProt:
  • Canonical: P03300 (Residues: 2-341; Coverage: 15%)
Sequence domains:
Structure domains:
Capsid protein VP1 Chain: 1
Molecule details ›
Chain: 1
Length: 302 amino acids
Theoretical weight: 33.49 KDa
Source organism: Human poliovirus 1 Mahoney
UniProt:
  • Canonical: P03300 (Residues: 580-881; Coverage: 14%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP3 Chain: 3
Molecule details ›
Chain: 3
Length: 238 amino acids
Theoretical weight: 26.55 KDa
Source organism: Human poliovirus 1 Mahoney
UniProt:
  • Canonical: P03300 (Residues: 342-579; Coverage: 11%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 322.9Å b: 358Å c: 380.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.281 not available not available