› 4nbv

X-ray diffraction
1.64Å resolution

Crystal structure of FabG from Cupriavidus taiwanensis

Released:
DOI: 10.2210/pdb4nbv/pdb
PDB entry 4nbv coloured by chain, front view.
PDB entry 4nbv coloured by chain, side view.
PDB entry 4nbv coloured by chain, top view.
Source organism: Cupriavidus taiwanensis
Primary publication:
Biochemical and structural studies of NADH-dependent FabG used to increase the bacterial production of fatty acids under anaerobic conditions.
Javidpour P, Pereira JH, Goh EB, McAndrew RP, Ma SM, Friedland GD, Keasling JD, Chhabra SR, Adams PD, Beller HR
Appl Environ Microbiol 80 497-505 (2014)
PMID: 24212572

Function and Biology Details

Reaction catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase putative short-chain dehydrogenases/reductases (SDR) family protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 25.77 KDa
Source organism: Cupriavidus taiwanensis
Expression system: Escherichia coli
UniProt:
  • Canonical: B3R6T4 (Residues: 1-246; Coverage: 100%)
Gene name: RALTA_A2639
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand B3P 1 x B3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P43212
Unit cell:
a: 111.763Å b: 111.763Å c: 79.198Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.136 0.154
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Metabolic engineering strategies for microbial synthesis of oleochemicals.
Pfleger et al. (2015)
6 more

2 mentions without citation

Biochemical and structural studies of NADH-dependent FabG used to increase the bacterial production of fatty acids under anaerobic conditions.
Javidpour et al. (2014)
1 more