Purification, crystallization and molecular symmetry of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis.
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.
Vogan
Erik M
EM
Department of Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA. vogan@crystal.harvard.edu
Bellamacina
Cornelia R
CR
He
Xuemei
X
Foxman
Bruce M
BM
Ringe
Dagmar
D
Liu
Hung-Wen
HW
Petsko
Gregory A
GA
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*
D006836:Hydro-Lyases; C089119:CDP-glucose 4,6-dehydratase