› 4qbb

X-ray diffraction
1.6Å resolution

Structure of the foot-and-mouth disease virus leader proteinase in complex with inhibitor (N~2~-[(3S)-4-({(2R)-1-[(4-CARBAMIMIDAMIDOBUTYL)AMINO]-4-METHYL-1-OXOPENTAN-2-YL}AMINO)-3-HYDROXY-4-OXOBUTANOYL]-L-ARGINYL-L-PROLINAMIDE)

Released:
DOI: 10.2210/pdb4qbb/pdb
PDB 4qbb coloured by chain and viewed from the front.
PDB 4qbb coloured by chain and viewed from the side.
PDB 4qbb coloured by chain and viewed from the top.
Source organism: Foot-and-mouth disease virus (strain O1)
Primary publication:
Foot-and-mouth disease virus leader proteinase: Structural insights into the mechanism of intermolecular cleavage.
Steinberger J, Grishkovskaya I, Cencic R, Juliano L, Juliano MA, Skern T
Virology 468-470C 397-408 (2014)
PMID: 25240326

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leader protease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Foot-and-mouth disease virus (strain O1)
Expression system: Escherichia coli
UniProt:
  • Canonical: P03305 (Residues: 29-195; Coverage: 7%)
Sequence domains: Foot-and-mouth virus L-proteinase
Structure domains: Cysteine proteinases

Ligands and Environments

3 bound ligands:
Ligand K 1 x K
Ligand E69 3 x E69
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 45.808Å b: 110.682Å c: 56.774Å
α: 90° β: 98.12° γ: 90°
R-values:
R R work R free
0.171 0.17 0.201
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Uncovering targets of the Leader protease: Linking RNA-mediated pathways and antiviral defense.
Saiz et al. (2021)
3 more

7 mentions without citation

Structure and Function of Viral Deubiquitinating Enzymes.
Bailey-Elkin et al. (2017)
6 more