Structure of dihydrouridine synthase C (DusC) from Escherichia coli

Minghao Chen, Jian Yu, Yoshikazu Tanaka, Miyuki Tanaka, Isao Tanaka, Min Yao

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

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 2.1Å 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.

Original languageEnglish
Pages (from-to)834-838
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number8
DOIs
Publication statusPublished - 2013 Aug
Externally publishedYes

Keywords

  • dihydrouridine
  • dihydrouridine synthase
  • tRNA modification

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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