› 4fq9

X-ray diffraction
2.02Å resolution

Crystal Structure of 3-hydroxydecanoyl-Acyl Carrier Protein Dehydratase (FabA) from Pseudomonas aeruginosa

Released:
DOI: 10.2210/pdb4fq9/pdb
PDB entry 4fq9 coloured by chain, front view.
PDB entry 4fq9 coloured by chain, side view.
PDB entry 4fq9 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural insights into the mechanism and inhibition of the β-hydroxydecanoyl-acyl carrier protein dehydratase from Pseudomonas aeruginosa.
Moynié L, Leckie SM, McMahon SA, Duthie FG, Koehnke A, Taylor JW, Alphey MS, Brenk R, Smith AD, Naismith JH
J Mol Biol 425 365-77 (2013)
PMID: 23174186

Function and Biology Details

Reactions catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H(2)O
Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 172 amino acids
Theoretical weight: 18.83 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: O33877 (Residues: 1-171; Coverage: 100%)
Gene names: PA1610, fabA
Sequence domains: FabA-like domain
Structure domains: Hotdog Thioesterase

Ligands and Environments

2 bound ligands:
Ligand PO4 10 x PO4
Ligand GOL 12 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 146.79Å b: 135.78Å c: 111.01Å
α: 90° β: 108.82° γ: 90°
R-values:
R R work R free
0.188 0.187 0.211
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal.
Cronan JE. (2014)
5 more

1 mention without citation

Structural analysis of the dual-function thioesterase SAV606 unravels the mechanism of Michael addition of glycine to an α,β-unsaturated thioester.
Chisuga et al. (2017)