Structure of dihydrouridine synthase C (DusC) from Escherichia coli

• Chen, Minghao

• Yu, Jian

• Tanaka, Yoshikazu

• Tanaka, Miyuki

• Tanaka, Isao

• Yao, Min

抄録

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 angstrom 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.

収録刊行物

• Acta Crystallographica Section F : Structural Biology And Crystallization Communications

  Acta Crystallographica Section F : Structural Biology And Crystallization Communications 69 (8), 834-838, 2013-08

  International Union of Crystallography

キーワード

• dihydrouridin
• dihydrouridine synthase
• tRNA modification

詳細情報

• CRID: 1050001339014429056
• NII論文ID: 120005317013
• HANDLE: 2115/53114
• ISSN: 17443091
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles