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Publication Abstract from PubMed

Dihydrouridine (D) is one of the most widely conserved tRNA modifications. Dihydrouridine synthase (Dus) is responsible for introducing D modifications into RNA by the reduction of uridine. Recently, a unique substrate-recognition mechanism using a small adapter molecule has been proposed for Thermus thermophilus Dus (TthDusC). To acquire insight regarding its substrate-recognition mechanism, the crystal structure of DusC from Escherichia coli (EcoDusC) was determined at 2.1 A resolution. EcoDusC was shown to be composed of two domains: an N-terminal catalytic domain and a C-terminal tRNA-binding domain. An L-shaped electron density surrounded by highly conserved residues was found in the active site, as observed for TthDus. Structure comparison with TthDus indicated that the N-terminal region has a similar structure, whereas the C-terminal domain has marked differences in its relative orientation to the N-terminal domain as well as in its own structure. These observations suggested that Dus proteins adopt a common substrate-recognition mechanism using an adapter molecule, whereas the manner of tRNA binding is diverse.

Structure of dihydrouridine synthase C (DusC) from Escherichia coli.,Chen M, Yu J, Tanaka Y, Tanaka M, Tanaka I, Yao M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):834-8. doi:, 10.1107/S1744309113019489. Epub 2013 Jul 27. PMID:23908023^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.