Crystallization and preliminary X-ray crystallographic analysis of γ-carboxymucolactone decarboxylase from Sulfolobus solfataricus

摘要

γ-Carboxymucolactone decarboxylase (γ-CMD; EC 4.1.1.44) catalyzes the conversion of γ-carboxymucolactone to β-ketoadipate enol-lactone in the β-­ketoadipate pathway, which is a key part of the degradation process of aromatic compounds in bacteria and in some eukaryotes such as fungi and yeast. γ-­CMD from the thermophilic archaeon Sulfolobus solfataricus (Ss γ-CMD) is encoded by the pcaC gene and is composed of 139 amino-acid residues with a molecular mass of 15 945 Da. Ss γ-CMD was crystallized and X-ray data were collected to 2.40 Å resolution. The crystal belonged to space group P43212, with unit-cell parameters a = b = 66.66, c = 184.82 Å. The Matthews coefficient and solvent content were estimated to be 2.14 ų Da⁻¹ and 42.6%, respectively, assuming that the asymmetric unit contained three recombinant protein molecules.