3koa

X-ray diffraction
2.4Å resolution

M296I mutant of foot-and-mouth disease virus RNA-polymerase in complex with a template- primer RNA and GTP

Released:

Function and Biology Details

Reactions catalysed:
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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192990 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
Macromolecules (3 distinct):
3D polymerase Chain: A
Molecule details ›
Chain: A
Length: 476 amino acids
Theoretical weight: 53.47 KDa
Source organism: Foot and mouth disease virus C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9QCE3 (Residues: 1858-2327; Coverage: 20%)
Sequence domains: Viral RNA-dependent RNA polymerase
Structure domains:
RNA (5'-R(P*AP*UP*GP*GP*GP*C)-3') Chain: B
Molecule details ›
Chain: B
Length: 6 nucleotides
Theoretical weight: 1.93 KDa
Source organism: Foot and mouth disease virus C
Expression system: Not provided
RNA (5'-R(P*CP*CP*CP*G)-3') Chain: C
Molecule details ›
Chain: C
Length: 4 nucleotides
Theoretical weight: 1.22 KDa
Source organism: Foot and mouth disease virus C
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3221
Unit cell:
a: 95.371Å b: 95.371Å c: 100.878Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.223 0.29
Expression systems:
  • Escherichia coli BL21
  • Not provided