Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5.
1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP(+) to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 A. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 A. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.
Jeyakanthan
Jeyaraman
J
National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan. kanthan@spring8.or.jp
Thamotharan
Subbiah
S
Panjikar
Santosh
S
Kitamura
Yoshiaki
Y
Nakagawa
Noriko
N
Shinkai
Akeo
A
Kuramitsu
Seiki
S
Yokoyama
Shigeyuki
S
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D055503:Protein Multimerization
D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C052370:1,3-propanediol dehydrogenase