› 2vc5

X-ray diffraction
2.6Å resolution

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

Released:
DOI: 10.2210/pdb2vc5/pdb
PDB entry 2vc5 coloured by chain, front view.
PDB entry 2vc5 coloured by chain, side view.
PDB entry 2vc5 coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Structural basis for natural lactonase and promiscuous phosphotriesterase activities.
Elias M, Dupuy J, Merone L, Mandrich L, Porzio E, Moniot S, Rochu D, Lecomte C, Rossi M, Masson P, Manco G, Chabriere E
J Mol Biol 379 1017-28 (2008)
PMID: 18486146

Function and Biology Details

Reaction catalysed: 
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aryldialkylphosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 35.66 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97VT7 (Residues: 1-314; Coverage: 100%)
Gene names: SSO2522, php
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

4 bound ligands:
Ligand FE2 4 x FE2
Ligand CO 4 x CO
Ligand EDO 15 x EDO
Ligand GOL 6 x GOL
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 87.16Å b: 104.82Å c: 155.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.282
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Quorum quenching: role in nature and applied developments.
Grandclément et al. (2016)
16 more

18 mentions without citation

Divergence and convergence in enzyme evolution: parallel evolution of paraoxonases from quorum-quenching lactonases.
Elias et al. (2012)
17 more