Crystallization and preliminary X-ray crystallographic analysis of malonyl-CoA decarboxylase from Rhizobium leguminosarum bv. trifolii.
Malonyl-CoA decarboxylase (MCD), which catalyzes the conversion of malonyl-CoA to acetyl-CoA, is an evolutionarily distinct and highly conserved enzyme. MCD does not share sequence homology with other known decarboxylases, while the enzymes from different species exhibit at least >30% sequence identity to each other. In order to provide a canonical structure of the enzyme for detailed study of its structure-function relationship, the MCD of Rhizobium leguminosarum bv. trifolii was overexpressed and crystallized. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 133.45, b = 127.10, c = 66.37 A. The asymmetric unit is likely to contain two molecules of MCD (molecular weight of 51 418 Da), with a crystal Volume per protein weight (V(M)) of 2.69 A(3) Da(-1) and a solvent content of about 54.3% by Volume. A native data set to 3.0 A resolution was obtained using a rotating-anode X-ray generator.
Jung
Jin-Seok
JS
National Creative Research Initiative Center for Biomolecular Recognition and Department of Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, South Korea.
Baek
Dong-Jin
DJ
Lee
Ga-Young
GY
Kim
Yu-Sam
YS
Oh
Byung-Ha
BH
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry; D016961:Rhizobium leguminosarum / Q000201:enzymology*
D011994:Recombinant Proteins; D002262:Carboxy-Lyases; C021532:malonyl-CoA decarboxylase