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.