› 2a4o

X-ray diffraction
1.55Å resolution

Dual modes of modification of Hepatitis A virus 3C protease by a serine derived beta-lactone: selective crytstallization and high resolution structure of the His102 adduct

Released:
DOI: 10.2210/pdb2a4o/pdb
PDB entry 2a4o coloured by chain, front view.
PDB entry 2a4o coloured by chain, side view.
PDB entry 2a4o coloured by chain, top view.
Source organism: Human hepatitis A virus Hu/Northern Africa/MBB/1978
Primary publication:
Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site.
Yin J, Bergmann EM, Cherney MM, Lall MS, Jain RP, Vederas JC, James MN
OpenAccess logo J Mol Biol 354 854-71 (2005)
PMID: 16288920

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.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146811 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.12 KDa
Source organism: Human hepatitis A virus Hu/Northern Africa/MBB/1978
Expression system: Escherichia coli
UniProt:
  • Canonical: P13901 (Residues: 1520-1738; Coverage: 10%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

4 bound ligands:
Ligand BBL 1 x BBL
Ligand ACE 1 x ACE
Ligand VAL 1 x VAL
Ligand NFA 1 x NFA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 43.914Å b: 56.072Å c: 81.293Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.198
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells.
Sun et al. (2016)
5 more

3 mentions without citation

Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site.
Yin et al. (2005)
2 more