title: Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5.
abstract: 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.
authors.affiliation: National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan. kanthan@spring8.or.jp
authors.forename: Jeyaraman
authors.initials: J
authors.lastname: Jeyakanthan
authors.forename: Subbiah
authors.initials: S
authors.lastname: Thamotharan
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Kitamura
authors.forename: Noriko
authors.initials: N
authors.lastname: Nakagawa
authors.forename: Akeo
authors.initials: A
authors.lastname: Shinkai
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: 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
chemical_list: D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C052370:1,3-propanediol dehydrogenase