title: Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Synechocystis sp. PCC 6803.
abstract: Malonyl-coenzymeA:acyl-carrier protein transacylase (MCAT), which catalyzes the transfer of the malonyl group from malonyl-CoA to acyl-carrier protein (ACP), is an essential enzyme in type II fatty-acid synthesis. The enzyme MCAT from Synechocystis sp. PCC 6803 (spMCAT), the first MCAT counterpart from a cyanobacterium, was cloned, purified and crystallized in order to determine its three-dimensional crystal structure. A higher-quality crystal with better diffraction was obtained by crystallization optimization. The crystal diffracted to 1.8 Å resolution and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 43.22, b = 149.21, c = 40.59 Å. Matthews coefficient calculations indicated that the crystal contained one spMCAT molecule in the asymmetric unit with a Matthews coefficient of 2.18 Å(3) Da(-1) and a solvent content of 43.65%.
authors.affiliation: Marine Bioproducts Engineering Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, People's Republic of China.
authors.forename: Yinghui
authors.initials: Y
authors.lastname: Liu
authors.forename: Yanming
authors.initials: Y
authors.lastname: Zhang
authors.forename: Xupeng
authors.initials: X
authors.lastname: Cao
authors.forename: Song
authors.initials: S
authors.lastname: Xue
mesh_terms: D051080:Acyl-Carrier Protein S-Malonyltransferase / Q000737:chemistry* / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D046939:Synechocystis / Q000201:enzymology*
chemical_list: D051080:Acyl-Carrier Protein S-Malonyltransferase
keywords: Synechocystis; malonyl-CoA:acyl-carrier protein transacylase (MCAT)