Open AccessCrystallization and preliminary X‐ray crystallographic analysis of γ‐carboxymucolactone decarboxylase from Sulfolobus solfataricus
Author(s) -
Lee Ho Yeon,
Yang Jin Kuk
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109042535
Subject(s) - sulfolobus solfataricus , thermophile , crystallization , crystallography , angstrom , stereochemistry , chemistry , crystal structure , molecule , monoclinic crystal system , solvent , recombinant dna , psychrophile , enzyme , archaea , biochemistry , gene , organic chemistry
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 P 4 3 2 1 2, with unit‐cell parameters a = b = 66.66, c = 184.82 Å. The Matthews coefficient and solvent content were estimated to be 2.14 Å 3 Da −1 and 42.6%, respectively, assuming that the asymmetric unit contained three recombinant protein molecules.