› 2fs2

X-ray diffraction
2Å resolution

Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon

Released:
DOI: 10.2210/pdb2fs2/pdb
PDB entry 2fs2 coloured by chain, front view.
PDB entry 2fs2 coloured by chain, side view.
PDB entry 2fs2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI.
Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD
J Biol Chem 281 11028-38 (2006)
PMID: 16464851

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160050 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A thioesterase PaaI Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 16.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P76084 (Residues: 2-140; Coverage: 99%)
Gene names: JW1391, b1396, paaI, ydbV
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P3121
Unit cell:
a: 69.847Å b: 69.847Å c: 117.168Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.23
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Microbial degradation of aromatic compounds - from one strategy to four.
Fuchs et al. (2011)
6 more

7 mentions without citation

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