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Purification, crystallization and molecular symmetry of CDP-D-glucose 4,6-dehydratase from Yersinia
Erik M Vogan1, Cornelia R Bellamacina, Xuemei He
1Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA. vogan@crystal.harvard.edu
Abstract:
The enzyme CDP-D-glucose 4,6-dehydratase (EC 4.2.1.45) is an NAD(+)-dependent oxidoreductase which catalyzes the irreversible conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. The product of this reaction is an intermediate in the synthesis of all CDP-linked 3,6-dideoxyhexoses, an important class of antigenic determinants found in the lipopolysaccharide layer of Gram-negative bacteria. Crystals of a recombinant form of this enzyme from Yersinia pseudotuberculosis have been grown in two crystal forms, both possessing pseudo-translational non-crystallographic symmetry, with dramatically different diffraction characteristics. A complete 1.8 A data set has been collected from the primitive orthorhombic crystal form, for which the non-crystallographic symmetry is described in detail.
