Crystallization and preliminary X-ray crystallographic analysis of gamma-carboxymucolactone decarboxylase from Sulfolobus solfataricus.
gamma-Carboxymucolactone decarboxylase (gamma-CMD; EC 4.1.1.44) catalyzes the conversion of gamma-carboxymucolactone to beta-ketoadipate enol-lactone in the beta-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. gamma-CMD from the thermophilic archaeon Sulfolobus solfataricus (Ss gamma-CMD) is encoded by the pcaC gene and is composed of 139 amino-acid residues with a molecular mass of 15 945 Da. Ss gamma-CMD was crystallized and X-ray data were collected to 2.40 angstrom resolution. The crystal belonged to space group P4(3)2(1)2, with unit-cell parameters a = b = 66.66, c = 184.82 angstrom. The Matthews coefficient and solvent content were estimated to be 2.14 angstrom(3) Da(-1) and 42.6%, respectively, assuming that the asymmetric unit contained three recombinant protein molecules.
Lee
Ho Yeon
HY
Department of Chemistry, Soongsil University, Seoul, Republic of Korea.
Yang
Jin Kuk
JK
D000272:Adipates / Q000737:chemistry; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D015394:Molecular Structure; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D014961:X-Ray Diffraction
D000272:Adipates; D019843:Archaeal Proteins; C027316:3-oxoadipic acid; D002262:Carboxy-Lyases; C019832:4-carboxymuconolactone decarboxylase