Molecular basis of dihydrouridine formation on tRNA
スポンサーリンク
概要
- 論文の詳細を見る
Dihydrouridine (D) is a highly conserved modified base found in tRNAs from all domains of life. Dihydrouridine synthase (Dus) catalyzes the D formation of tRNA through reduction of uracil base with flavin mononucleotide (FMN) as a cofactor. Here, we report the crystal structures of Thermus thermophilus Dus (TthDus), which is responsible for D formation at positions 20 and 20a, in complex with tRNA and with a short fragment of tRNA (D-loop). Dus interacts extensively with the D-arm and recognizes the elbow region composed of the kissing loop interaction between T- and D-loops in tRNA, pulling U20 into the catalytic center for reduction. Although distortion of the D-loop structure was observed upon binding of Dus to tRNA, the canonical D-loop/T-loop interaction was maintained. These results were consistent with the observation that Dus preferentially recognizes modified rather than unmodified tRNAs, indicating that Dus introduces D20 by monitoring the complete L-shaped structure of tRNAs. In the active site, U20 is stacked on the isoalloxazine ring of FMN, and C5 of the U20 uracil ring is covalently cross-linked to the thiol group of Cys93, implying a catalytic mechanism of D20 formation. In addition, the involvement of a cofactor molecule in uracil ring recognition was proposed. Based on a series of mutation analyses, we propose a molecular basis of tRNA recognition and D formation catalyzed by Dus.
- National Academy of Sciencesの論文
- 2011-12-06
著者
関連論文
- 1P326 Structural analysis of uro-adherence factor A, UafA, from Staphylococcus saprophyticus(11. Morphogenesis and cell adhesion,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P016 Structural analysis of EbhA from Staphylococcus aureus(1. Protein structure and dynamics (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P017 Crystal structure and molecular characterization of NEAT domain from Staphylococcus aureus(1. Protein structure and dynamics (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- A Review on Prolate Spheroidal Wave Functions
- 3D1358 The Recognition Mechanism of eIF2β for its partner proteins eIF5 and eIF2β_ε(3D Protein: Structure & Function 3,The 49th Annual Meeting of the Biophysical Society of Japan)
- Molecular basis of dihydrouridine formation on tRNA