title: Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA.
abstract: Dihydrouridine synthase (Dus) is responsible for catalyzing dihydrouridine formation in RNA by the reduction of uridine. To elucidate its RNA-recognition mechanism, Dus from Thermus thermophilus (TthDus) and its complex with tRNA were crystallized. Diffraction data sets were collected from crystals of native and selenomethionine-substituted TthDus to resolutions of 1.70 and 2.30 Å, respectively. These crystals belonged to space group P1. Preliminary X-ray crystallographic analysis showed that two molecules of TthDus were contained in an asymmetric unit. In addition, diffraction data were collected to 3.51 Å resolution from a crystal of selenomethionine-substituted TthDus in complex with tRNA, which belonged to space group P4(1)2(1)2. Preliminary structural analysis showed that the asymmetric unit contained two TthDus-tRNA complexes.
authors.affiliation: Graduate School of Life Sciences, Hokkaido University, Sapporo, Japan.
authors.forename: Futao
authors.initials: F
authors.lastname: Yu
authors.forename: Yoshikazu
authors.initials: Y
authors.lastname: Tanaka
authors.forename: Shiho
authors.initials: S
authors.lastname: Yamamoto
authors.forename: Akiyoshi
authors.initials: A
authors.lastname: Nakamura
authors.forename: Shunsuke
authors.initials: S
authors.lastname: Kita
authors.forename: Nagisa
authors.initials: N
authors.lastname: Hirano
authors.forename: Isao
authors.initials: I
authors.lastname: Tanaka
authors.forename: Min
authors.initials: M
authors.lastname: Yao
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010088:Oxidoreductases / Q000737:chemistry*; D012343:RNA, Transfer / Q000737:chemistry*; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D012343:RNA, Transfer; D010088:Oxidoreductases; C462500:tRNA-dihydrouridine synthase