› 5tic

X-ray diffraction
1.65Å resolution

X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5

Released:
DOI: 10.2210/pdb5tic/pdb
PDB entry 5tic coloured by chain, front view.
PDB entry 5tic coloured by chain, side view.
PDB entry 5tic coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids.
Grisewood MJ, Hernandez Lozada NJ, Thoden JB, Gifford NP, Mendez-Perez D, Schoenberger HA, Allan MF, Floy ME, Lai RY, Holden HM, Pfleger BF, Maranas CD
ACS Catal 7 3837-3849 (2017)
PMID: 29375928

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioesterase 1/protease 1/lysophospholipase L1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 185 amino acids
Theoretical weight: 20.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ADA1 (Residues: 28-208; 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 CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 40.922Å b: 82.124Å c: 53.903Å
α: 90° β: 90.44° γ: 90°
R-values:
R R work R free
0.188 0.186 0.222
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Protein Engineering for Improving and Diversifying Natural Product Biosynthesis.
Li et al. (2020)
5 more

6 mentions without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)
5 more