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 P41212. Preliminary structural analysis showed that the asymmetric unit contained two TthDus-tRNA complexes.
Original language | English |
---|---|
Pages (from-to) | 685-688 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 67 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2011 Jun 1 |
Externally published | Yes |
Keywords
- Thermus thermophilus
- dihydrouridine synthase
- flavin mononucleotide
- tRNA
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics