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.

SUBMITTER: Yu F 

PROVIDER: S-EPMC3107143 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature