Open AccessCrystallization and preliminary X‐ray characterization of 1,3‐propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
Author(s) -
Marçal D.,
Rego A. T.,
Fogg M. J.,
Wilson K. S.,
Carrondo M. A.,
Enguita F. J.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107008834
Subject(s) - klebsiella pneumoniae , escherichia coli , 1,3 propanediol , crystallization , orthorhombic crystal system , 2,3 butanediol , dehydrogenase , glycerol , chemistry , microbiology and biotechnology , crystallography , nuclear chemistry , biology , enzyme , biochemistry , crystal structure , gene , organic chemistry , fermentation
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 P 2 1 , with unit‐cell parameters a = 91.9, b = 226.6, c = 232.6 Å, β = 92.9°. The crystals probably contain two decamers in the asymmetric unit, with a V M value of 3.07 Å 3 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.