Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Staphylococcus aureus
- Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Staphylococcus aureus
- 홍승곤; 김국한; 김은경
- Issue Date
- Acta crystallographica. Section F, Structural biology and crystallization communications [electronic serial]
- VOL 66, 20-22
- Malonyl-CoA:acyl-carrier protein transacylase (MCAT), encoded by the fabd
gene, is a key enzyme in type II fatty-acid biosynthesis. It is responsible for
transferring the malonyl group from malonyl-CoA to the holo acyl-carrier
protein (ACP). Since the type II system differs from the type I system that
mammals use, it has received enormous attention as a possible antibiotic target.
In particular, only a single isoform of MCAT has been reported and a
continuous coupled enzyme assay has been developed. MCAT from Staphylococcus
aureus was overexpressed in Escherichia coli and the protein was purified
and crystallized. Diffraction data were collected to 1.2 A ° resolution. The crystals
belonged to space group P21, with unit-cell parameters a = 41.608, b = 86.717,
c = 43.163 A ° , α = γ = 90, β = 106.330 °. The asymmetric unit contains one
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