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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1197-9. doi: 10.1107/S1744309109042535. Epub 2009 Oct 30.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipates / chemistry
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Molecular Structure
  • Sulfolobus solfataricus / enzymology*
  • X-Ray Diffraction

Substances

  • Adipates
  • Archaeal Proteins
  • 3-oxoadipic acid
  • Carboxy-Lyases
  • 4-carboxymuconolactone decarboxylase