› 1j00

X-ray diffraction
2Å resolution

E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety

Released:
DOI: 10.2210/pdb1j00/pdb
PDB entry 1j00 coloured by chain, front view.
PDB entry 1j00 coloured by chain, side view.
PDB entry 1j00 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network.
Lo YC, Lin SC, Shaw JF, Liaw YC
J Mol Biol 330 539-51 (2003)
PMID: 12842470

Function and Biology Details

Reactions catalysed: 
A phenyl acetate + H(2)O = a phenol + acetate
2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate
Palmitoyl-CoA + H(2)O = CoA + palmitate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-142338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioesterase 1/protease 1/lysophospholipase L1 Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ADA1 (Residues: 27-208; Coverage: 100%)
Gene names: JW0483, apeA, b0494, pldC, tesA
Sequence domains: GDSL-like Lipase/Acylhydrolase
Structure domains: SGNH hydrolase

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand SDP 1 x SDP

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL17B2
Spacegroup: P43212
Unit cell:
a: 49.907Å b: 49.907Å c: 171.898Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

GDSL family of serine esterases/lipases.
Akoh et al. (2004)
4 more

6 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
5 more