Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

crystallization communications

Acta Cryst. (2007). F63, 249-251 [ doi:10.1107/S1744309107008834 ]

Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae

D. Marçal, A. T. Rego, M. J. Fogg, K. S. Wilson, M. A. Carrondo and F. J. Enguita

Abstract: 1,3-Propanediol dehydrogenase (1,3-PD-DH), encoded by the dhaT gene, is a key enzyme in the dissimilation process for converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae. Single colourless crystals were obtained from a recombinant preparation of 1,3-propanediol dehydrogenase overexpressed in Escherichia coli. The crystals belong to space group P2₁, with unit-cell parameters a = 91.9, b = 226.6, c = 232.6 Å, [beta] = 92.9°. The crystals probably contain two decamers in the asymmetric unit, with a V_M value of 3.07 Å³ Da^-1 and an estimated solvent content of 59%. Diffraction data were collected to 2.7 Å resolution using synchrotron radiation at the ID14-4 beamline of the European Synchrotron Radiation Facility.

Keywords: 1,3-propanediol dehydrogenase; Klebsiella pneumoniae; glycerol metabolism; KES; opportunistic pathogens.