title: Purification, crystallization and molecular symmetry of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis.
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.
authors.affiliation: Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA. vogan@crystal.harvard.edu
authors.forename: Erik M
authors.initials: EM
authors.lastname: Vogan
authors.forename: Cornelia R
authors.initials: CR
authors.lastname: Bellamacina
authors.forename: Xuemei
authors.initials: X
authors.lastname: He
authors.forename: Bruce M
authors.initials: BM
authors.lastname: Foxman
authors.forename: Dagmar
authors.initials: D
authors.lastname: Ringe
authors.forename: Hung-Wen
authors.initials: HW
authors.lastname: Liu
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Petsko
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry*; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D011487:Protein Conformation; D015011:Yersinia pseudotuberculosis / Q000201:enzymology*
chemical_list: D006836:Hydro-Lyases; C089119:CDP-glucose 4,6-dehydratase