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Structure of dihydrouridine synthase C (DusC) from Escherichia coli

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Title: Structure of dihydrouridine synthase C (DusC) from Escherichia coli
Authors: Chen, Minghao Browse this author
Yu, Jian Browse this author
Tanaka, Yoshikazu Browse this author →KAKEN DB
Tanaka, Miyuki Browse this author
Tanaka, Isao Browse this author →KAKEN DB
Yao, Min Browse this author →KAKEN DB
Keywords: dihydrouridin
dihydrouridine synthase
tRNA modification
Issue Date: Aug-2013
Publisher: International Union of Crystallography
Journal Title: Acta Crystallographica Section F : Structural Biology And Crystallization Communications
Volume: 69
Issue: 8
Start Page: 834
End Page: 838
Publisher DOI: 10.1107/S1744309113019489
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 2.1 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.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田中 良和

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