Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Staphylococcus aureus

Title
Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Staphylococcus aureus
Authors
홍승곤김국한김은경
Issue Date
2010-01
Publisher
Acta crystallographica. Section F, Structural biology and crystallization communications [electronic serial]
Citation
VOL 66, 20-22
Abstract
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 SaMCAT molecule.
URI
http://pubs.kist.re.kr/handle/201004/38311
ISSN
1744-3091
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