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Cloning, preliminary characterization and crystallization of nucleoside hydrolases from Caenorhabditis elegans and Campylobacter jejuni

2003; Wiley; Volume: 59; Issue: 6 Linguagem: Inglês

10.1107/s0907444903007078

1399-0047

Wim Versées, Els Van Holsbeke, S. De Vos, Klaas Decanniere, Ingrid Zegers, Jan Steyaert,

Porphyrin Metabolism and Disorders

The nucleoside hydrolases (NHs) are a family of nucleoside-modifying enzymes. They play an important role in the purine-salvage pathway of many pathogenic organisms which are unable to synthesize purines de novo. Although well characterized in protozoan parasites, their precise function and mechanism remain unclear in other species. For the first time, NHs from Caenorhabditis elegans and Campylobacter jejuni, which are representatives of mesozoa and bacteria, respectively, have been cloned and purified. Steady-state kinetics indicate a different substrate-specificity profile to previously described hydrolases. Native diffraction data sets were collected from crystals of NH from each organism. The hexagonal crystals (space group P6222 or P6422) of NH from C. elegans diffracted to a resolution of 2.8 Å, while the data set from the orthorhombic crystals (space group I222 or I212121) of NH from C. jejuni could be processed to 1.7 Å resolution. The unit-cell parameters were a = b = 102.23, c = 117.27 Å in the former case and a = 101.13, b = 100.13, c = 81.37 Å in the latter.