Open AccessCloning, purification, crystallization and preliminary X‐ray crystallographic analysis of MCAT from Staphylococcus aureus
Author(s) -
Hong Seung Kon,
Kim Kook Han,
Kim Eunice EunKyeong
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109045989
Subject(s) - crystallization , staphylococcus aureus , cloning (programming) , crystallography , x ray , materials science , microbiology and biotechnology , chemistry , biology , physics , bacteria , genetics , optics , computer science , organic chemistry , programming language
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 Å resolution. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 41.608, b = 86.717, c = 43.163 Å, α = γ = 90, β = 106.330°. The asymmetric unit contains one Sa MCAT molecule.