› 3sj7

X-ray diffraction
2.5Å resolution

Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH

Released:
DOI: 10.2210/pdb3sj7/pdb
PDB entry 3sj7 coloured by chain, front view.
PDB entry 3sj7 coloured by chain, side view.
PDB entry 3sj7 coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Primary publication:
Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal FabG1 in positive cooperativity for NADPH.
Dutta D, Bhattacharyya S, Das AK
Proteins 80 1250-7 (2012)
PMID: 22275129

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 26.88 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli M15
UniProt:
  • Canonical: Q2FZ53 (Residues: 1-244; Coverage: 100%)
Gene name: SAOUHSC_01199
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
Ligand PG4 3 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: R32
Unit cell:
a: 126.484Å b: 126.484Å c: 176.954Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.177 0.253
Expression system: Escherichia coli M15

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Citations

1 review citation

Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents.
Wang et al. (2013)
12 other articles

6 mentions without citation

Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.
Haft et al. (2017)
5 more