1fmd

X-ray diffraction
3.5Å resolution

THE STRUCTURE AND ANTIGENICITY OF A TYPE C FOOT-AND-MOUTH DISEASE VIRUS

Released:
Model geometry
Fit model/data
Data not deposited

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.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero 240-mer (preferred)
PDBe Complex ID:
PDB-CPX-147207 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Foot and mouth disease virus VP1 capsid protein Chain: 1
Molecule details ›
Chain: 1
Length: 208 amino acids
Theoretical weight: 22.69 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: Q65095 (Residues: 1-208; Coverage: 100%)
Sequence domains: Picornavirus coat protein
Structure domains: Jelly Rolls
Capsid protein VP2 Chain: 2
Molecule details ›
Chain: 2
Length: 218 amino acids
Theoretical weight: 24.3 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P15072 (Residues: 287-504; Coverage: 9%)
Sequence domains: picornavirus capsid protein
Structure domains: Jelly Rolls
Capsid protein VP3 Chain: 3
Capsid protein VP4 Chain: 4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: I23
Unit cell:
a: 347.6Å b: 347.6Å c: 347.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 not available
Expression system: Mesocricetus auratus