6gvv

X-ray diffraction
2.35Å resolution

Mutant M16A of RNA dependent RNA polymerase 3D from Foot-and-Mouth disease Virus

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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-.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase 3D-POL Chain: A
Molecule details ›
Chain: A
Length: 481 amino acids
Theoretical weight: 54.05 KDa
Source organism: Foot and mouth disease virus C
Expression system: Escherichia coli
UniProt:
  • Canonical: P03311 (Residues: 1858-2327; Coverage: 20%)
Sequence domains: Viral RNA-dependent RNA polymerase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 93.12Å b: 93.12Å c: 121.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.263
Expression system: Escherichia coli